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Conserved domains on  [gi|893570856|ref|NP_001297618|]
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GPI ethanolamine phosphate transferase 2 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
62-335 1.84e-158

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: 1.84e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  62 PPLFSKVVIVLIDALRDDFVFGSKgvKYMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPV 141
Cdd:cd16024    1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 142 LLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRGDWDVLILHYLGLDHI 221
Cdd:cd16024   79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 222 GHISGPNSPLIGHKLSEMDSVLMKIHTSLLSKdrETLLPSLLVLCGDHGMSETGSHGASSTEEVSTPLLLISSAFERKP- 300
Cdd:cd16024  159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQ--SSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 893570856 301 ---GDIRHPKHVQQTDLAATLAIGLGLPIPKDSVGSLL 335
Cdd:cd16024  237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
PIGO_PIGG super family cl44747
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
811-965 2.65e-17

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.


The actual alignment was detected with superfamily member pfam19316:

Pssm-ID: 437148  Cd Length: 423  Bit Score: 85.72  E-value: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  811 RPHNLPVLAFSLLIQTVMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATIDISAGFVGLDTYMEVPATFLTVF 890
Cdd:pfam19316 252 RATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGYNVVAVGVLTFV 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  891 GTYVGPVLWASHLVYFLSSEGNNSALSRSCFCYALICSVPVATYIVLV----TSLRYHLFIWSVFSPKLLYE-----GMH 961
Cdd:pfam19316 327 SNWAGPIWWTSATNLLLLRKRRRGEGRGVFFQHLALLTLFVAASLVSVmaacTALRTHLFIWTVFSPKYLYTmawslGQH 406

                  ....
gi 893570856  962 LLIT 965
Cdd:pfam19316 407 LLVN 410
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
62-335 1.84e-158

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: 1.84e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  62 PPLFSKVVIVLIDALRDDFVFGSKgvKYMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPV 141
Cdd:cd16024    1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 142 LLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRGDWDVLILHYLGLDHI 221
Cdd:cd16024   79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 222 GHISGPNSPLIGHKLSEMDSVLMKIHTSLLSKdrETLLPSLLVLCGDHGMSETGSHGASSTEEVSTPLLLISSAFERKP- 300
Cdd:cd16024  159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQ--SSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 893570856 301 ---GDIRHPKHVQQTDLAATLAIGLGLPIPKDSVGSLL 335
Cdd:cd16024  237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
PIGO_PIGG pfam19316
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
811-965 2.65e-17

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: 85.72  E-value: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  811 RPHNLPVLAFSLLIQTVMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATIDISAGFVGLDTYMEVPATFLTVF 890
Cdd:pfam19316 252 RATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGYNVVAVGVLTFV 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  891 GTYVGPVLWASHLVYFLSSEGNNSALSRSCFCYALICSVPVATYIVLV----TSLRYHLFIWSVFSPKLLYE-----GMH 961
Cdd:pfam19316 327 SNWAGPIWWTSATNLLLLRKRRRGEGRGVFFQHLALLTLFVAASLVSVmaacTALRTHLFIWTVFSPKYLYTmawslGQH 406

                  ....
gi 893570856  962 LLIT 965
Cdd:pfam19316 407 LLVN 410
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
67-274 1.51e-15

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 79.41  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  67 KVVIVLIDALRDDFVfgskGVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------------- 129
Cdd:COG1524   25 KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwydpelg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 130 -------FVDVIRNLNSPVLLEDnVLRQAKAAGKRIIFYGdetWVKLFPKHFVEY------DGTTSFFvsDYIEVDKNVT 196
Cdd:COG1524   98 rvvnslsWVEDGFGSNSLLPVPT-IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLL--GNPAADRWIA 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 893570856 197 RHLDKVLKRGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSET 274
Cdd:COG1524  172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDV 247
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
68-279 2.43e-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: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856   68 VVIVLIDALRDDFVFGskgVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVDvirnlNS--- 139
Cdd:pfam01663   1 LLVISLDGFRADYLDR---FELTPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPgshGIVG-----NTfyd 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  140 PVLLEDNVLRQAKAAGKRiiFYGDE-TWVKL-----------FP---KHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLK 204
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPR--WWQGEpIWDTAakagvraaalfWPgseVDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  205 ------------RGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMS 272
Cdd:pfam01663 148 qtwldlpfadvaAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMT 225

                  ....*..
gi 893570856  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 1.84e-158

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: 1.84e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  62 PPLFSKVVIVLIDALRDDFVFGSKgvKYMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPV 141
Cdd:cd16024    1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 142 LLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRGDWDVLILHYLGLDHI 221
Cdd:cd16024   79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 222 GHISGPNSPLIGHKLSEMDSVLMKIHTSLLSKdrETLLPSLLVLCGDHGMSETGSHGASSTEEVSTPLLLISSAFERKP- 300
Cdd:cd16024  159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLEEQ--SSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 893570856 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 4.33e-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: 4.33e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  62 PPLFSKVVIVLIDALRDDFVFGSKGVKY----------MPYTTYLVEKGASHS----FVAEakPPTVTMPRIKALMTGSL 127
Cdd:cd16023    1 PPRFDKVVLLLIDALRYDFVLPDDENPPsenslyyhnkLPVLEELLKSQPNNSrlfkFIAD--PPTTTLQRLKGLTTGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 128 PGFVDVIRNLNSPVLLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRG- 206
Cdd:cd16023   79 PTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 207 DWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIhTSLLSKDretllpSLLVLCGDHGMSETGSHGASSTEEVS 286
Cdd:cd16023  159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDI-IERLDDD------TLLLVFGDHGMTETGDHGGDSDEEVD 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 893570856 287 TPLLLIS---------SAFERKPGDIRHPKHVQQTDLAATLAIGLGLPIPKDSVGSL 334
Cdd:cd16023  232 AALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTV 288
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
62-332 6.56e-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: 6.56e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  62 PPLFSKVVIVLIDALRDDFVF-----GSKGVKYMpytTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRN 136
Cdd:cd16019    1 PTKYDKVVLIVIDGLRYDLAVnvnkqSSFFSFLQ---KLNEQPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 137 LNSPVLLEDNVLRQAKAAGKRIIFYGDETWVKLFPKHFVEYDGTTSFFVSDYIEVDKNVTRHL----DKVLKRGDWDVLI 212
Cdd:cd16019   78 FASSEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHIndnlDENIYYDNWDFII 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 213 LHYLGLDHIGHISG-PNSPLIGHKLSEMDSVLMKIHTSlLSKDRetllpsLLVLCGDHGMSETGSHGASSTEEVSTPLLL 291
Cdd:cd16019  158 LHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDR-MDNDT------LLVVVSDHGMNNDGNHGGSSTEETSSFFFF 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 893570856 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 4.72e-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: 4.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  62 PPLFSKVVIVLIDALRDDFVFGSKGvKYMPYTTYLVEK----GASHSFVaeakpPTVTMPRIKALMTGSlpgFVD---VI 134
Cdd:cd16020    1 PPPAKRLVVFVADGLRADTFFENNC-SRAPFLRKIFLNqglwGISHTRV-----PTESRPGHVALFAGF---YEDpsaVT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 135 RNLNS-PVLLeDNVLRQAKAAgkriIFYGDETWVKLFPK------HFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLKRGD 207
Cdd:cd16020   72 KGWKEnPVEF-DSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLANAS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 208 WD----------VLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLLS--KDRET--LLPSllvlcgDHGMSE 273
Cdd:cd16020  147 SNktellnqdglVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTayIFTS------DHGMTD 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893570856 274 TGSHGASSTEEVSTPLLL-----------ISSAFERKPGDIRHPKH-VQQTDLAATLAIGLGLPIPKDSVGSL 334
Cdd:cd16020  221 WGSHGDGSPDETETPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
PIGO_PIGG pfam19316
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
811-965 2.65e-17

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: 85.72  E-value: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  811 RPHNLPVLAFSLLIQTVMTkfiwkPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATIDISAGFVGLDTYMEVPATFLTVF 890
Cdd:pfam19316 252 RATNIPLFLLFRLQLEFLS-----SLDLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGYNVVAVGVLTFV 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  891 GTYVGPVLWASHLVYFLSSEGNNSALSRSCFCYALICSVPVATYIVLV----TSLRYHLFIWSVFSPKLLYE-----GMH 961
Cdd:pfam19316 327 SNWAGPIWWTSATNLLLLRKRRRGEGRGVFFQHLALLTLFVAASLVSVmaacTALRTHLFIWTVFSPKYLYTmawslGQH 406

                  ....
gi 893570856  962 LLIT 965
Cdd:pfam19316 407 LLVN 410
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
66-278 1.15e-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: 81.09  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  66 SKVVIVLIDALRDDFVfgSKGvKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVD---VIRNL 137
Cdd:cd16018    1 PPLIVISIDGFRWDYL--DRA-GLTPNLKRLAEEGVR---AKYVKPvfPTLTFPNHYSIVTGLYPeshGIVGnyfYDPKT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 138 NSPVLLEDNVLR-----------QAKAAGKR-------------IIFYGDETWVKLFPKHFveYDGTTSFFVSDYIEVDK 193
Cdd:cd16018   75 NEEFSDSDWVWDpwwiggepiwvTAEKAGLKtasyfwpgsevaiIGYNPTPIPLGGYWQPY--NDSFPFEERVDTILEWL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 194 NVTRHldkvlkrgdwDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSE 273
Cdd:cd16018  153 DLERP----------DLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEAL--KERGLLDDTNIIVVSDHGMTD 220

                 ....*
gi 893570856 274 TGSHG 278
Cdd:cd16018  221 VGTHG 225
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
67-274 1.51e-15

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 79.41  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  67 KVVIVLIDALRDDFVfgskGVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------------- 129
Cdd:COG1524   25 KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGLYPGehgivgngwydpelg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 130 -------FVDVIRNLNSPVLLEDnVLRQAKAAGKRIIFYGdetWVKLFPKHFVEY------DGTTSFFvsDYIEVDKNVT 196
Cdd:COG1524   98 rvvnslsWVEDGFGSNSLLPVPT-IFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDGRKPLL--GNPAADRWIA 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 893570856 197 RHLDKVLKRGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSET 274
Cdd:COG1524  172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYEGTLVIVTADHGMVDV 247
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
68-319 3.59e-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: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  68 VVIVLIDALRDDFVFgsKGVKYMPYTTYLvEKGASHSFVAEAK---PPTVTMPRIKALMTGSLPGFVDVIRNLnspvllE 144
Cdd:cd00016    3 VVLIVLDGLGADDLG--KAGNPAPTTPNL-KRLASEGATFNFRsvsPPTSSAPNHAALLTGAYPTLHGYTGNG------S 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 145 DNVLRQAKAAGKRIIFYgdeTWVKLFPKHFVEydgTTSFFVSDYIEVDKNvtrhldkvlkrGDWDVLILHYLGLDHIGHI 224
Cdd:cd00016   74 ADPELPSRAAGKDEDGP---TIPELLKQAGYR---TGVIGLLKAIDETSK-----------EKPFVLFLHFDGPDGPGHA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 225 SGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMSETGSHGA--------SSTEEVSTPLLLISSAF 296
Cdd:cd00016  137 YGPNTPEYYDAVEEIDERIGKVLDAL--KKAGDADDTVIIVTADHGGIDKGHGGDpkadgkadKSHTGMRVPFIAYGPGV 214
                        250       260
                 ....*....|....*....|...
gi 893570856 297 eRKPGDIRHPkhVQQTDLAATLA 319
Cdd:cd00016  215 -KKGGVKHEL--ISQYDIAPTLA 234
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
68-279 2.43e-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: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856   68 VVIVLIDALRDDFVFGskgVKYMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVDvirnlNS--- 139
Cdd:pfam01663   1 LLVISLDGFRADYLDR---FELTPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPgshGIVG-----NTfyd 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  140 PVLLEDNVLRQAKAAGKRiiFYGDE-TWVKL-----------FP---KHFVEYDGTTSFFVSDYIEVDKNVTRHLDKVLK 204
Cdd:pfam01663  70 PKTGEYLVFVISDPEDPR--WWQGEpIWDTAakagvraaalfWPgseVDYSTYYGTPPRYLKDDYNNSVPFEDRVDTAVL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  205 ------------RGDWDVLILHYLGLDHIGHISGPNSPLIGHKLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMS 272
Cdd:pfam01663 148 qtwldlpfadvaAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMT 225

                  ....*..
gi 893570856  273 ETGSHGA 279
Cdd:pfam01663 226 PVSDDKV 232
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
67-337 1.30e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 54.09  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856  67 KVVIVLIDALRDDFV-FGSKGVKYMPYTTYLVEKGA------SHSfvaeakPPTvtMPRIKALMTGSLP---GFVDVIRN 136
Cdd:cd16148    2 NVILIVIDSLRADHLgCYGYDRVTTPNLDRLAAEGVvfdnhySGS------NPT--LPSRFSLFTGLYPfyhGVWGGPLE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 137 LNSPVLLEdnVLRQAkaaGKRIIFYGDETWVKLFP------KHFVEYDGTTSFFVSDYIEVDKNVTRH----LDKVLKRG 206
Cdd:cd16148   74 PDDPTLAE--ILRKA---GYYTAAVSSNPHLFGGPgfdrgfDTFEDFRGQEGDPGEEGDERAERVTDRalewLDRNADDD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 207 DWdVLILHYlgldhighisgpNSPligH-------KLSEMDSVLMKIHTSLlsKDRETLLPSLLVLCGDHGMS-----ET 274
Cdd:cd16148  149 PF-FLFLHY------------FDP---HepylydaEVRYVDEQIGRLLDKL--KELGLLEDTLVIVTSDHGEEfgehgLY 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 893570856 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 4.62e-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: 4.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 250 LLSKDRETLLPSLLVLCGDHGMSeTGSH-----GASSTEEVS-TPLLLISSAFERKPGDIRHPkhVQQTDLAATLAIGLG 323
Cdd:cd16156  257 VLDAADEIAEDAWVIYTSDHGDM-LGAHklwakGPAVYDEITnIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAG 333
                         90       100
                 ....*....|....*....|...
gi 893570856 324 LPIPKDSVGSLLFPVIEGKPMRE 346
Cdd:cd16156  334 IPQPKVLEGESILATIEDPEIPE 356
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
251-336 1.24e-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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893570856 251 LSKDRETLLpslLVLCGDHGmSETGSHGASST-----EEVSTPLLLISSAFERKPGDIRHPKHVQQTDLAATL--AIGLG 323
Cdd:cd16153  193 LKQDRDYTI---VYVTGDHG-WHLGEQGILAKftfwpQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLlaAAGVD 268
                         90
                 ....*....|...
gi 893570856 324 LPIPKDSVGSLLF 336
Cdd:cd16153  269 VDAPDYLDGRDLF 281
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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