|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
62-335 |
7.92e-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: 467.04 E-value: 7.92e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 62 PPLFSKVVIVLIDALRDDFVFGSKgvKYMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPV 141
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 142 LLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRGDWDVLILHYLGLDHI 221
Cdd:cd16024 79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 222 GHISGPNSPLIGHKLSEMDSVLMKIHTSLLSKdrETLLPSLLVLCGDHGMSETGSHGASSTEEVSTPLLLISSAFERKP- 300
Cdd:cd16024 159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQ--SSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 1690504810 301 ---GDIRHPKHVQQTDLAATLAIGLGLPIPKDSVGSLL 335
Cdd:cd16024 237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
67-274 |
1.12e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 79.79 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 67 KVVIVLIDALRDDFVfgskGVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------------- 129
Cdd:COG1524 25 KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwydpelg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 130 -------FVDVIRNLNSPVLLEDnVLRQAKAAGKRIIFYGdetWVKLFPKHFVEY------DGTTSFFvsDYIEVDKNVT 196
Cdd:COG1524 98 rvvnslsWVEDGFGSNSLLPVPT-IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLL--GNPAADRWIA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1690504810 197 RHLDKVLKRGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSET 274
Cdd:COG1524 172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDV 247
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
68-279 |
2.06e-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: 60.13 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 68 VVIVLIDALRDDFVFGskgVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVDvirnlNS--- 139
Cdd:pfam01663 1 LLVISLDGFRADYLDR---FELTPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPgshGIVG-----NTfyd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 140 PVLLEDNVLRQAKAAGKRiiFYGDE-TWVKL-----------FP---KHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLK 204
Cdd:pfam01663 70 PKTGEYLVFVISDPEDPR--WWQGEpIWDTAakagvraaalfWPgseVDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 205 ------------RGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMS 272
Cdd:pfam01663 148 qtwldlpfadvaAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMT 225
|
....*..
gi 1690504810 273 ETGSHGA 279
Cdd:pfam01663 226 PVSDDKV 232
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
62-335 |
7.92e-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: 467.04 E-value: 7.92e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 62 PPLFSKVVIVLIDALRDDFVFGSKgvKYMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPV 141
Cdd:cd16024 1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 142 LLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRGDWDVLILHYLGLDHI 221
Cdd:cd16024 79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 222 GHISGPNSPLIGHKLSEMDSVLMKIHTSLLSKdrETLLPSLLVLCGDHGMSETGSHGASSTEEVSTPLLLISSAFERKP- 300
Cdd:cd16024 159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQ--SSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 1690504810 301 ---GDIRHPKHVQQTDLAATLAIGLGLPIPKDSVGSLL 335
Cdd:cd16024 237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
62-334 |
7.19e-95 |
|
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: 7.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 62 PPLFSKVVIVLIDALRDDFVFGSKGVKY----------MPYTTYLVEKGASHS----FVAEakPPTVTMPRIKALMTGSL 127
Cdd:cd16023 1 PPRFDKVVLLLIDALRYDFVLPDDENPPsenslyyhnkLPVLEELLKSQPNNSrlfkFIAD--PPTTTLQRLKGLTTGSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 128 PGFVDVIRNLNSPVLLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRG- 206
Cdd:cd16023 79 PTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 207 DWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIhTSLLSKDretllpSLLVLCGDHGMSETGSHGASSTEEVS 286
Cdd:cd16023 159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDI-IERLDDD------TLLLVFGDHGMTETGDHGGDSDEEVD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1690504810 287 TPLLLIS---------SAFERKPGDIRHPKHVQQTDLAATLAIGLGLPIPKDSVGSL 334
Cdd:cd16023 232 AALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTV 288
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
62-332 |
1.63e-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: 242.65 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 62 PPLFSKVVIVLIDALRDDFVF-----GSKGVKYMpytTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRN 136
Cdd:cd16019 1 PTKYDKVVLIVIDGLRYDLAVnvnkqSSFFSFLQ---KLNEQPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 137 LNSPVLLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHL----DKVLKRGDWDVLI 212
Cdd:cd16019 78 FASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHIndnlDENIYYDNWDFII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 213 LHYLGLDHIGHISG-PNSPLIGHKLSEMDSVLMKIHTSlLSKDRetllpsLLVLCGDHGMSETGSHGASSTEEVSTPLLL 291
Cdd:cd16019 158 LHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDR-MDNDT------LLVVVSDHGMNNDGNHGGSSTEETSSFFFF 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1690504810 292 IS-SAFERKPGDIRHPKHVQ-----------------QTDLAATLAIGLGLPIPKDSVG 332
Cdd:cd16019 231 ISkKGFFKKRPIDQIEKIKQnneqqkidpseyiriiyQIDILPTICYLLGIPIPFNNIG 289
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
62-334 |
4.00e-24 |
|
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: 103.44 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 62 PPLFSKVVIVLIDALRDDFVFGSKGvKYMPYTTYLVEK----GASHSFVaeakpPTVTMPRIKALMTGSlpgFVD---VI 134
Cdd:cd16020 1 PPPAKRLVVFVADGLRADTFFENNC-SRAPFLRKIFLNqglwGISHTRV-----PTESRPGHVALFAGF---YEDpsaVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 135 RNLNS-PVLLeDNVLRQAKAAgkriIFYGDETWVKLFPK------HFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRGD 207
Cdd:cd16020 72 KGWKEnPVEF-DSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLANAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 208 WD----------VLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLLS--KDRET--LLPSllvlcgDHGMSE 273
Cdd:cd16020 147 SNktellnqdglVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTayIFTS------DHGMTD 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1690504810 274 TGSHGASSTEEVSTPLLL-----------ISSAFERKPGDIRHPKH-VQQTDLAATLAIGLGLPIPKDSVGSL 334
Cdd:cd16020 221 WGSHGDGSPDETETPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
66-278 |
7.49e-17 |
|
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: 81.48 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 66 SKVVIVLIDALRDDFVfgSKGvKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVD---VIRNL 137
Cdd:cd16018 1 PPLIVISIDGFRWDYL--DRA-GLTPNLKRLAEEGVR---AKYVKPvfPTLTFPNHYSIVTGLYPeshGIVGnyfYDPKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 138 NSPVLLEDNVLR-----------QAKAAGKR-------------IIFYGDETWVKLFPKHFveYDGTTSFFVSDYIEVDK 193
Cdd:cd16018 75 NEEFSDSDWVWDpwwiggepiwvTAEKAGLKtasyfwpgsevaiIGYNPTPIPLGGYWQPY--NDSFPFEERVDTILEWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 194 NVTRHldkvlkrgdwDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSE 273
Cdd:cd16018 153 DLERP----------DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEAL--KERGLLDDTNIIVVSDHGMTD 220
|
....*
gi 1690504810 274 TGSHG 278
Cdd:cd16018 221 VGTHG 225
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
67-274 |
1.12e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 79.79 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 67 KVVIVLIDALRDDFVfgskGVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------------- 129
Cdd:COG1524 25 KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwydpelg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 130 -------FVDVIRNLNSPVLLEDnVLRQAKAAGKRIIFYGdetWVKLFPKHFVEY------DGTTSFFvsDYIEVDKNVT 196
Cdd:COG1524 98 rvvnslsWVEDGFGSNSLLPVPT-IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLL--GNPAADRWIA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1690504810 197 RHLDKVLKRGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSET 274
Cdd:COG1524 172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDV 247
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
68-319 |
3.08e-15 |
|
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: 75.92 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 68 VVIVLIDALRDDFVFgsKGVKYMPYTTYLvEKGASHSFVAEAK---PPTVTMPRIKALMTGSLPGFVDVIRNLnspvllE 144
Cdd:cd00016 3 VVLIVLDGLGADDLG--KAGNPAPTTPNL-KRLASEGATFNFRsvsPPTSSAPNHAALLTGAYPTLHGYTGNG------S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 145 DNVLRQAKAAGKRIIFYgdeTWVKLFPKHFVEydgTTSFFVSDYIEVDKNvtrhldkvlkrGDWDVLILHYLGLDHIGHI 224
Cdd:cd00016 74 ADPELPSRAAGKDEDGP---TIPELLKQAGYR---TGVIGLLKAIDETSK-----------EKPFVLFLHFDGPDGPGHA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 225 SGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSETGSHGA--------SSTEEVSTPLLLISSAF 296
Cdd:cd00016 137 YGPNTPEYYDAVEEIDERIGKVLDAL--KKAGDADDTVIIVTADHGGIDKGHGGDpkadgkadKSHTGMRVPFIAYGPGV 214
|
250 260
....*....|....*....|...
gi 1690504810 297 eRKPGDIRHPkhVQQTDLAATLA 319
Cdd:cd00016 215 -KKGGVKHEL--ISQYDIAPTLA 234
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
68-279 |
2.06e-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: 60.13 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 68 VVIVLIDALRDDFVFGskgVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVDvirnlNS--- 139
Cdd:pfam01663 1 LLVISLDGFRADYLDR---FELTPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPgshGIVG-----NTfyd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 140 PVLLEDNVLRQAKAAGKRiiFYGDE-TWVKL-----------FP---KHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLK 204
Cdd:pfam01663 70 PKTGEYLVFVISDPEDPR--WWQGEpIWDTAakagvraaalfWPgseVDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 205 ------------RGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMS 272
Cdd:pfam01663 148 qtwldlpfadvaAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMT 225
|
....*..
gi 1690504810 273 ETGSHGA 279
Cdd:pfam01663 226 PVSDDKV 232
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
67-337 |
9.48e-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: 54.48 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 67 KVVIVLIDALRDDFV-FGSKGVKYMPYTTYLVEKGA------SHSfvaeakPPTvtMPRIKALMTGSLP---GFVDVIRN 136
Cdd:cd16148 2 NVILIVIDSLRADHLgCYGYDRVTTPNLDRLAAEGVvfdnhySGS------NPT--LPSRFSLFTGLYPfyhGVWGGPLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 137 LNSPVLLEdnVLRQAkaaGKRIIFYGDETWVKLFP------KHFVEYDGTTSFFVSDYIEVDKNVTRH----LDKVLKRG 206
Cdd:cd16148 74 PDDPTLAE--ILRKA---GYYTAAVSSNPHLFGGPgfdrgfDTFEDFRGQEGDPGEEGDERAERVTDRalewLDRNADDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 207 DWdVLILHYlgldhighisgpNSPligH-------KLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMS-----ET 274
Cdd:cd16148 149 PF-FLFLHY------------FDP---HepylydaEVRYVDEQIGRLLDKL--KELGLLEDTLVIVTSDHGEEfgehgLY 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1690504810 275 GSHGASSTEEVS-TPLLLissAFERKPGDIRHPKHVQQTDLAATLAIGLGLPIPKDSVGSLLFP 337
Cdd:cd16148 211 WGHGSNLYDEQLhVPLII---RWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
250-346 |
3.96e-04 |
|
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: 43.91 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 250 LLSKDRETLLPSLLVLCGDHGMSeTGSH-----GASSTEEVS-TPLLLISSAFERKPGDIRHPkhVQQTDLAATLAIGLG 323
Cdd:cd16156 257 VLDAADEIAEDAWVIYTSDHGDM-LGAHklwakGPAVYDEITnIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAG 333
|
90 100
....*....|....*....|...
gi 1690504810 324 LPIPKDSVGSLLFPVIEGKPMRE 346
Cdd:cd16156 334 IPQPKVLEGESILATIEDPEIPE 356
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
251-336 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690504810 251 LSKDRETLLpslLVLCGDHGmSETGSHGASST-----EEVSTPLLLISSAFERKPGDIRHPKHVQQTDLAATL--AIGLG 323
Cdd:cd16153 193 LKQDRDYTI---VYVTGDHG-WHLGEQGILAKftfwpQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLlaAAGVD 268
|
90
....*....|...
gi 1690504810 324 LPIPKDSVGSLLF 336
Cdd:cd16153 269 VDAPDYLDGRDLF 281
|
|
| |
