|
Name |
Accession |
Description |
Interval |
E-value |
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
12-265 |
1.95e-36 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 136.80 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 12 LLLCSYQMIAQEDRQKEKKLVFIIVDGIAADMIPKTSTPNLDAISLKGDFSEAYvgggkgtYSETPTISAVGYNSLLTGV 91
Cdd:COG1524 7 LLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPL-------TSVFPSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 92 WVNKHNVYGNEIKQPNY--------------------NYPSIF-RLFTNDFPekqTAIFSTWEDNRTKLLGENlvgtnfl 150
Cdd:COG1524 80 YPGEHGIVGNGWYDPELgrvvnslswvedgfgsnsllPVPTIFeRARAAGLT---TAAVFWPSFEGSGLIDAA------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 151 kIDYAFDGfEKDTLNFPHDpyreyikniDKKVAYQAAEYIQNEAPDLTWVYLEFSDDMGHGYG-DSPQLYNAITFEDELI 229
Cdd:COG1524 150 -RPYPYDG-RKPLLGNPAA---------DRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGpDSPEYRAALREVDAAL 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 294983029 230 GKIYEAIKyrESNFNEDWLFIVTTDHGRTAKDGKRH 265
Cdd:COG1524 219 GRLLDALK--ARGLYEGTLVIVTADHGMVDVPPDID 252
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
29-305 |
9.21e-21 |
|
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: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 29 KKLVFIIVDGIAADMIPKTS-TPNLDAISLKGdfseAYVGGGKGTYsetPTISAVGYNSLLTGVWVNKHNVYGNEIKQPN 107
Cdd:cd16018 1 PPLIVISIDGFRWDYLDRAGlTPNLKRLAEEG----VRAKYVKPVF---PTLTFPNHYSIVTGLYPESHGIVGNYFYDPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 108 YNypSIFRLFTNDFP-------------EKQ---TAIFsTWednrtkllgenlVGTNFLKIDYAFDGFEKDTLNFPHDPY 171
Cdd:cd16018 74 TN--EEFSDSDWVWDpwwiggepiwvtaEKAglkTASY-FW------------PGSEVAIIGYNPTPIPLGGYWQPYNDS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 172 REYiknidKKVAYQAAEYIQNEAPDLTWVYLEFSDDMGHGYG-DSPQLYNAITFEDELIGKIYEAIKyrESNFNEDWLFI 250
Cdd:cd16018 139 FPF-----EERVDTILEWLDLERPDLILLYFEEPDSAGHKYGpDSPEVNEALKRVDRRLGYLIEALK--ERGLLDDTNII 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294983029 251 VTTDHGRTAKdGKrHGGQSDRE--RSTWIAMNKkgnsYFKEQ--IPGI--VDILPTMISFL 305
Cdd:cd16018 212 VVSDHGMTDV-GT-HGYDNELPdmRAIFIARGP----AFKKGkkLGPFrnVDIYPLMCNLL 266
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
31-256 |
1.35e-18 |
|
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: 86.32 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 31 LVFIIVDGIAADMIPK-TSTPNLDAISLKGDfseayvgGGKGTYSETPTISAVGYNSLLTGVWVNKHNVYGNEIKQPNYN 109
Cdd:pfam01663 1 LLVISLDGFRADYLDRfELTPNLAALAKEGV-------SAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 110 YPSIFRLFTNDFPE--KQTAIFSTWEDNRTKllgenlVGTNFL---KIDYAFDGFEKDTlnFPHDPYR---EYIKNIDKK 181
Cdd:pfam01663 74 EYLVFVISDPEDPRwwQGEPIWDTAAKAGVR------AAALFWpgsEVDYSTYYGTPPR--YLKDDYNnsvPFEDRVDTA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 182 VAYQ----AAEYIQNEAPDLTWVYLEFSDDMGHGYG-DSPQLYNAITFEDELIGKIYEAIKyrESNFNEDWLFIVTTDHG 256
Cdd:pfam01663 146 VLQTwldlPFADVAAERPDLLLVYLEEPDYAGHRYGpDSPEVEDALRRVDRAIGDLLEALD--ERGLFEDTNVIVVSDHG 223
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
12-265 |
1.95e-36 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 136.80 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 12 LLLCSYQMIAQEDRQKEKKLVFIIVDGIAADMIPKTSTPNLDAISLKGDFSEAYvgggkgtYSETPTISAVGYNSLLTGV 91
Cdd:COG1524 7 LLLASLLAAAAAAAPPAKKVVLILVDGLRADLLERAHAPNLAALAARGVYARPL-------TSVFPSTTAPAHTTLLTGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 92 WVNKHNVYGNEIKQPNY--------------------NYPSIF-RLFTNDFPekqTAIFSTWEDNRTKLLGENlvgtnfl 150
Cdd:COG1524 80 YPGEHGIVGNGWYDPELgrvvnslswvedgfgsnsllPVPTIFeRARAAGLT---TAAVFWPSFEGSGLIDAA------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 151 kIDYAFDGfEKDTLNFPHDpyreyikniDKKVAYQAAEYIQNEAPDLTWVYLEFSDDMGHGYG-DSPQLYNAITFEDELI 229
Cdd:COG1524 150 -RPYPYDG-RKPLLGNPAA---------DRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGpDSPEYRAALREVDAAL 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 294983029 230 GKIYEAIKyrESNFNEDWLFIVTTDHGRTAKDGKRH 265
Cdd:COG1524 219 GRLLDALK--ARGLYEGTLVIVTADHGMVDVPPDID 252
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
29-305 |
9.21e-21 |
|
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: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 29 KKLVFIIVDGIAADMIPKTS-TPNLDAISLKGdfseAYVGGGKGTYsetPTISAVGYNSLLTGVWVNKHNVYGNEIKQPN 107
Cdd:cd16018 1 PPLIVISIDGFRWDYLDRAGlTPNLKRLAEEG----VRAKYVKPVF---PTLTFPNHYSIVTGLYPESHGIVGNYFYDPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 108 YNypSIFRLFTNDFP-------------EKQ---TAIFsTWednrtkllgenlVGTNFLKIDYAFDGFEKDTLNFPHDPY 171
Cdd:cd16018 74 TN--EEFSDSDWVWDpwwiggepiwvtaEKAglkTASY-FW------------PGSEVAIIGYNPTPIPLGGYWQPYNDS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 172 REYiknidKKVAYQAAEYIQNEAPDLTWVYLEFSDDMGHGYG-DSPQLYNAITFEDELIGKIYEAIKyrESNFNEDWLFI 250
Cdd:cd16018 139 FPF-----EERVDTILEWLDLERPDLILLYFEEPDSAGHKYGpDSPEVNEALKRVDRRLGYLIEALK--ERGLLDDTNII 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294983029 251 VTTDHGRTAKdGKrHGGQSDRE--RSTWIAMNKkgnsYFKEQ--IPGI--VDILPTMISFL 305
Cdd:cd16018 212 VVSDHGMTDV-GT-HGYDNELPdmRAIFIARGP----AFKKGkkLGPFrnVDIYPLMCNLL 266
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
31-256 |
1.35e-18 |
|
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: 86.32 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 31 LVFIIVDGIAADMIPK-TSTPNLDAISLKGDfseayvgGGKGTYSETPTISAVGYNSLLTGVWVNKHNVYGNEIKQPNYN 109
Cdd:pfam01663 1 LLVISLDGFRADYLDRfELTPNLAALAKEGV-------SAPNLTPVFPTLTFPNHYTLVTGLYPGSHGIVGNTFYDPKTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 110 YPSIFRLFTNDFPE--KQTAIFSTWEDNRTKllgenlVGTNFL---KIDYAFDGFEKDTlnFPHDPYR---EYIKNIDKK 181
Cdd:pfam01663 74 EYLVFVISDPEDPRwwQGEPIWDTAAKAGVR------AAALFWpgsEVDYSTYYGTPPR--YLKDDYNnsvPFEDRVDTA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 182 VAYQ----AAEYIQNEAPDLTWVYLEFSDDMGHGYG-DSPQLYNAITFEDELIGKIYEAIKyrESNFNEDWLFIVTTDHG 256
Cdd:pfam01663 146 VLQTwldlPFADVAAERPDLLLVYLEEPDYAGHRYGpDSPEVEDALRRVDRAIGDLLEALD--ERGLFEDTNVIVVSDHG 223
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
29-323 |
1.49e-13 |
|
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: 70.27 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 29 KKLVFIIVDGIAADMI-----PKTSTPNLDAISLKG-DFSEAYVGGgkgtyseTPTISAVGynSLLTGVWVNKHNVYGne 102
Cdd:cd16148 1 MNVILIVIDSLRADHLgcygyDRVTTPNLDRLAAEGvVFDNHYSGS-------NPTLPSRF--SLFTGLYPFYHGVWG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 103 iKQPNYNYPSIFRLFT-NDFpekQTAIFSTWednrtkllGENLVGTNFlkiDYAFDGFEKDTLNFPHDPYREYIKniDKK 181
Cdd:cd16148 70 -GPLEPDDPTLAEILRkAGY---YTAAVSSN--------PHLFGGPGF---DRGFDTFEDFRGQEGDPGEEGDER--AER 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 182 VAYQAAEYIQNEAPDLTW-VYLEFSDdmGHGygdsPQLY-NAITFEDELIGKIYEAIKyrESNFNEDWLFIVTTDHGRTA 259
Cdd:cd16148 133 VTDRALEWLDRNADDDPFfLFLHYFD--PHE----PYLYdAEVRYVDEQIGRLLDKLK--ELGLLEDTLVIVTSDHGEEF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 260 KDgkrHGgqsdrerstwiAMNKKGNSYFKEQI--------PGI------------VDILPTMISFLELypetSVKEELDG 319
Cdd:cd16148 205 GE---HG-----------LYWGHGSNLYDEQLhvpliirwPGKepgkrvdalvshIDIAPTLLDLLGV----EPPDYSDG 266
|
....
gi 294983029 320 VPLL 323
Cdd:cd16148 267 RSLL 270
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
1-323 |
1.81e-09 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 59.12 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 1 MKFKITSMAMMLLlcsyqmiAQEDRQKEKK--LVFIIVDGIAADMI-----PKTSTPNLDAISLKG-DFSEAYVGGGkgt 72
Cdd:COG3119 1 MKRLLLLLLALLA-------AAAAAAAAKRpnILFILADDLGYGDLgcygnPLIKTPNIDRLAAEGvRFTNAYVTSP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 73 ySETPTISavgynSLLTGVWVNKHNVYGNeikqpNYNYPSIFRLFTNDFPEK------QTAIFSTWEDNRTKLLGENLVg 146
Cdd:COG3119 71 -VCSPSRA-----SLLTGRYPHRTGVTDN-----GEGYNGGLPPDEPTLAELlkeagyRTALFGKWHLYLTDLLTDKAI- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 147 tNFLKidyafDGFEKD-----TLNF--PHDPY---REYIKNIDKKVAYQAAEYIQNEAPDLTWvylefsDDMGHGYGDSp 216
Cdd:COG3119 139 -DFLE-----RQADKDkpfflYLAFnaPHAPYqapEEYLDKYDGKDIPLPPNLAPRDLTEEEL------RRARAAYAAM- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 217 qlynaITFEDELIGKIYEAIKyrESNFNEDWLFIVTTDHGRTAKD-GKRHGGQSDRERST-------WIAMNKKGNSYfk 288
Cdd:COG3119 206 -----IEEVDDQVGRLLDALE--ELGLADNTIVVFTSDNGPSLGEhGLRGGKGTLYEGGIrvplivrWPGKIKAGSVS-- 276
|
330 340 350
....*....|....*....|....*....|....*
gi 294983029 289 EQIPGIVDILPTMISFLELypetSVKEELDGVPLL 323
Cdd:COG3119 277 DALVSLIDLLPTLLDLAGV----PIPEDLDGRSLL 307
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
26-311 |
1.04e-08 |
|
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: 56.21 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 26 QKEKKLVFIIVDGIAADMIPKTS--TPNLDAI----SLKGDFSEAYvgggkgTYSETPTISAVGYNSLLTGVWVN----K 95
Cdd:cd16019 2 TKYDKVVLIVIDGLRYDLAVNVNkqSSFFSFLqklnEQPNNSFLAL------SFADPPTVTGPRLKALTTGNPPTfldlI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 96 HNVYGNEIKQPNY------NYPSIfrLFTND------FPEkqtaIFSTWEDNRTKLLGENLVGTNFlkidyafdgfekdt 163
Cdd:cd16019 76 SNFASSEIKEDNIirqlkkNGKKI--LFYGDdtwldlFPE----IFTYKFTITSFNIRDMHDVDPI-------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 164 lnfphdPYREYIKNIDKKVAYQAAEYIQNeapdltwvYLEFSDDMGHGYGD--SPQLYNAITFEDELIGKIYEAIkyres 241
Cdd:cd16019 136 ------FYNHINDNLDENIYYDNWDFIIL--------HFLGLDHLGHKHNTtsSPELEKKLDQMDNLIRDIYDRM----- 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294983029 242 nfNEDWLFIVTTDHGRTAKdgKRHGGQSDRERSTWI-AMNKKGNSYFK--EQIPGIVDILPTMISFLELYPET 311
Cdd:cd16019 197 --DNDTLLVVVSDHGMNND--GNHGGSSTEETSSFFfFISKKGFFKKRpiDQIEKIKQNNEQQKIDPSEYIRI 265
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
201-313 |
4.20e-08 |
|
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: 54.11 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 201 YLEFsDDMGHGYGDSPQLYNAITFE-DELIGKIYEAIKYRESNfnEDWLFIVTTDHGRTakDGKRHGGQSDRERST-WIA 278
Cdd:cd16024 152 YLGL-DHIGHLEGPKSPLMPPKLKEmDDVIKRIYESLEEQSSN--NPTLLVVCGDHGMT--DAGNHGGSSPGETSVpLLF 226
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 294983029 279 MNKKGNSYFKEQIPGI--------VDILPTMISFLEL-YPETSV 313
Cdd:cd16024 227 ISPKFSSKPSNADGELsyyetvqqVDLAPTLALLLGLpIPKNSV 270
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
29-301 |
7.51e-08 |
|
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: 52.81 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 29 KKLVFIIVDGIAADMIPKT-----STPNLDAISlkgdfSEAYVGGGKGTYseTPTISAVGYNSLLTGVWVNKHNVYGNEI 103
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAgnpapTTPNLKRLA-----SEGATFNFRSVS--PPTSSAPNHAALLTGAYPTLHGYTGNGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 104 KQPNYNYPSIFRlfTNDFPekqtaifSTWEDNRTKllgenlvgtnflkiDYAFDGFEkdtlnfphdpyreyiknidkkvA 183
Cdd:cd00016 74 ADPELPSRAAGK--DEDGP-------TIPELLKQA--------------GYRTGVIG----------------------L 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 184 YQAAEYIQNEAPDLTWVYLEFSDDMGHGYGDSPQLY-NAITFEDELIGKIYEAIKyrESNFNEDWLFIVTTDHGRTAKdG 262
Cdd:cd00016 109 LKAIDETSKEKPFVLFLHFDGPDGPGHAYGPNTPEYyDAVEEIDERIGKVLDALK--KAGDADDTVIIVTADHGGIDK-G 185
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 294983029 263 KRHGGQSDRERSTW-------IAMNKKGNSYFKEQIPGI--VDILPTM 301
Cdd:cd00016 186 HGGDPKADGKADKShtgmrvpFIAYGPGVKKGGVKHELIsqYDIAPTL 233
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-323 |
6.23e-07 |
|
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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 51.00 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 31 LVFIIVD-------GIAADmiPKTSTPNLDAISLKGD-FSEAYvgggkgtyseTPT-ISAVGYNSLLTGVWVNKHNVYGN 101
Cdd:cd16037 3 ILIIMSDehnpdamGCYGH--PVVRTPNLDRLAARGTrFENAY----------TPSpICVPSRASFLTGRYVHETGVWDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 102 EIKQPNyNYPSIFRLFTNdfpekqtaifstwEDNRTKLLGenlvGTNFLKIDYaFDGFEKDtlnfphdpyreyiknidKK 181
Cdd:cd16037 71 ADPYDG-DVPSWGHALRA-------------AGYETVLIG----KLHFRGEDQ-RHGFRYD-----------------RD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 182 VAYQAAEYIQNEAPDLT-WV-YLEFSD------------DMGH-----GYgdspqlYNAITFEDELIGKIYEAIKyrESN 242
Cdd:cd16037 115 VTEAAVDWLREEAADDKpWFlFVGFVAphfpliapqefyDLYVrraraAY------YGLVEFLDENIGRVLDALE--ELG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 243 FNEDWLFIVTTDHGRTAKDGKRHGGQSDRERSTWIAMNKKGNSYFKEQI---P-GIVDILPTMISFLelypETSVKEELD 318
Cdd:cd16037 187 LLDNTLIIYTSDHGDMLGERGLWGKSTMYEESVRVPMIISGPGIPAGKRvktPvSLVDLAPTILEAA----GAPPPPDLD 262
|
....*
gi 294983029 319 GVPLL 323
Cdd:cd16037 263 GRSLL 267
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-323 |
1.54e-06 |
|
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: 49.91 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 31 LVFIIVDGIAADMI-----PKTSTPNLDAISLKG-DFSEAYvgggkgtyseTPT-ISAVGYNSLLTGVWVNKHNVYGNEi 103
Cdd:cd16033 3 ILFIMTDQQRYDTLgcygnPIVKTPNIDRLAAEGvRFTNAY----------TPSpVCCPARASLLTGLYPHEHGVLNNV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 104 kqpnYNYPSIFR-------LFTNDFPEK--QTAIFSTWEdnrtkllgenlVGTNFLKIDYAFDGF--------------- 159
Cdd:cd16033 72 ----ENAGAYSRglppgveTFSEDLREAgyRNGYVGKWH-----------VGPEETPLDYGFDEYlpvettieyfladra 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 160 --------EKD-----TLNF--PHDPYreyiknidkkvaYQAAEYIQNEAPDLTWVYLEFSDDMGhgygDSPQLYNA--- 221
Cdd:cd16033 137 iemleelaADDkpfflRVNFwgPHDPY------------IPPEPYLDMYDPEDIPLPESFADDFE----DKPYIYRRerk 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 222 ----------------------ITFEDELIGKIYEAIKyrESNFNEDWLFIVTTDHGRTAkdGKrHGgqsdrerstwiaM 279
Cdd:cd16033 201 rwgvdtedeedwkeiiahywgyITLIDDAIGRILDALE--ELGLADDTLVIFTSDHGDAL--GA-HR------------L 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294983029 280 NKKGNSYFKE--QIPGIV-------------------DILPTmisFLELYpETSVKEELDG---VPLL 323
Cdd:cd16033 264 WDKGPFMYEEtyRIPLIIkwpgviaagqvvdefvsllDLAPT---ILDLA-GVDVPPKVDGrslLPLL 327
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
32-324 |
2.58e-06 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 49.04 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 32 VFIIVDGIAADMI----PKTSTPNLDAISLKG-DFSEAYVGGGkgtySETPTISAvgynsLLTGVWVNKHNVYGNEikQP 106
Cdd:cd16027 4 LWIIADDLSPDLGgyggNVVKTPNLDRLAAEGvRFTNAFTTAP----VCSPSRSA-----LLTGLYPHQNGAHGLR--SR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 107 NYNYPSIFRLFTNDFPEK--QTAIFS-TWEDNRTKLLGENLVGTNFLKIDYAFDGFEKDT---------------LNFpH 168
Cdd:cd16027 73 GFPLPDGVKTLPELLREAgyYTGLIGkTHYNPDAVFPFDDEMRGPDDGGRNAWDYASNAAdflnrakkgqpfflwFGF-H 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 169 DPYREYIKNIDKKVAYQAAE-----YIqneaPDLtwvyLEFSDDMGhgygdspQLYNAITFEDELIGKIYEAIKyrESNF 243
Cdd:cd16027 152 DPHRPYPPGDGEEPGYDPEKvkvppYL----PDT----PEVREDLA-------DYYDEIERLDQQVGEILDELE--EDGL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 244 NEDWLFIVTTDHGRTAKDGKRHGGqsdrERSTWIAM------NKKGNSYFKEQIPGIvDILPTMISFLELypetSVKEEL 317
Cdd:cd16027 215 LDNTIVIFTSDHGMPFPRAKGTLY----DSGLRVPLivrwpgKIKPGSVSDALVSFI-DLAPTLLDLAGI----EPPEYL 285
|
....*..
gi 294983029 318 DGVPLLG 324
Cdd:cd16027 286 QGRSFLP 292
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
31-256 |
4.55e-06 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 48.19 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 31 LVFIIVDGIAADMI-----PKTSTPNLDAISLKG-DFSEAYVGGGKGTYSETptisavgynSLLTGVWVNKHNVYGNEIK 104
Cdd:pfam00884 3 VVLVLGESLRAPDLglygyPRPTTPFLDRLAEEGlLFSNFYSGGTLTAPSRF---------ALLTGLPPHNFGSYVSTPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 105 QPNYNYPSIFRLFtndfpeKQ----TAIFSTWE---DNRTKllGENLVGTNFLKIDYAFDGFEKDTLNFPHDPYREYIkn 177
Cdd:pfam00884 74 GLPRTEPSLPDLL------KRagynTGAIGKWHlgwYNNQS--PCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGVS-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 178 iDKKVAYQAAEYIQNEAPD--LTWVYL----------EFSDDMGHGYGDSPQL-------YNAITFEDELIGKIYEAIKy 238
Cdd:pfam00884 144 -DEALLDEALEFLDNNDKPffLVLHTLgshgppyypdRYPEKYATFKPSSCSEeqllnsyDNTLLYTDDAIGRVLDKLE- 221
|
250
....*....|....*...
gi 294983029 239 rESNFNEDWLFIVTTDHG 256
Cdd:pfam00884 222 -ENGLLDNTLVVYTSDHG 238
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
29-275 |
8.85e-05 |
|
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: 44.12 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 29 KKLVFIIVDGIAADMI---PKTSTPNLDAISLKgdfsEAYVGGGKgtySETPTISAVGYNSLLTGvwvnkhnvygneikq 105
Cdd:cd16020 5 KRLVVFVADGLRADTFfenNCSRAPFLRKIFLN----QGLWGISH---TRVPTESRPGHVALFAG--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 106 pnynypsifrlftndFPEKQTAIFSTWED---------NRTK-------------LLGENLVGTNFLKIDYAFDGFEKDT 163
Cdd:cd16020 63 ---------------FYEDPSAVTKGWKEnpvefdsvfNRSRrswawgspdilpmFPKGATGGKVLTYIYPEEDFDSTDA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 164 lnfphdpyreyiKNIDKKVAYQAAEYIQNEAPDLT----------WVYLEFSDDMGHGYG-DSPQLYNAITFEDELIGKI 232
Cdd:cd16020 128 ------------SELDEWVFDKVEEFLANASSNKTellnqdglvfFLHLLGLDTNGHAHKpYSKEYLENIRYVDKGIEKT 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 294983029 233 YEAIKyresNFNED--WLFIVTTDHGRTakDGKRHGGQSDRERST 275
Cdd:cd16020 196 YPLIE----EYFNDgrTAYIFTSDHGMT--DWGSHGDGSPDETET 234
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
167-327 |
1.84e-03 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 40.25 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 167 PHDPY---REYIkniDKkvayqaaeYIQNEApdltwvylefsddmgHGYgdspqlYNAITFEDELIGKIYEAIKyrESNF 243
Cdd:cd16032 144 PHDPYvipQEYW---DL--------YVRRAR---------------RAY------YGMVSYVDDKVGQLLDTLE--RTGL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 244 NEDWLFIVTTDHGrtakD--GkrhggqsdrERSTWIAMnkkgnSYFK--EQIPGI------------------VDILPTM 301
Cdd:cd16032 190 ADDTIVIFTSDHG----DmlG---------ERGLWYKM-----SFFEgsARVPLIisapgrfaprrvaepvslVDLLPTL 251
|
170 180
....*....|....*....|....*.
gi 294983029 302 ISFLELYPETSVkEELDGVPLLGMVD 327
Cdd:cd16032 252 VDLAGGGTAPHV-PPLDGRSLLPLLE 276
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
209-305 |
2.86e-03 |
|
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: 39.47 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294983029 209 GHGYG-DSPQLYNAITFEDELIGKIYEAIkyresnfNEDWLFIVTTDHGRTAK-DgkrHGGQSDRE-RSTWIAMNKKGNS 285
Cdd:cd16023 174 GHRYGpNHPEMARKLTQMDQFIRDIIERL-------DDDTLLLVFGDHGMTETgD---HGGDSDEEvDAALFAYSKRPFN 243
|
90 100 110
....*....|....*....|....*....|...
gi 294983029 286 YFKEQIPGI-------------VDILPTmISFL 305
Cdd:cd16023 244 NSDEPIESNgpgdpskvrsvpqIDLVPT-LSLL 275
|
|
| |
