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Conserved domains on  [gi|688584443|ref|XP_009305959|]
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GPI ethanolamine phosphate transferase 2 isoform X2 [Danio rerio]

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 ...
66-335 1.94e-165

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: 484.76  E-value: 1.94e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  66 FKRVVIVLIDALREDFVFSSNgrRFMPYTRHVVEKGSSHSFIAKARPPTVTMPRIKALTTGSIPGFIDVVMNLNSPVLLE 145
Cdd:cd16024    4 FDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 146 DNLIWQAKSAGKRIIFYGDDTWVRLFPKHFMEQDGTTSFFVSDYTEVDNNVTRHLDSTLKRDDWDILILHYLGLDHIGHI 225
Cdd:cd16024   82 DNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 226 SGPHSSLIGPKLMEMDDIIKKIHASLisKESEGTLPNLLVVCGDHGMSETGSHGGSSEQEINTALVLISPAFRRKVGLER 305
Cdd:cd16024  162 EGPKSPLMPPKLKEMDDVIKRIYESL--EEQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPSNAD 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 688584443 306 -----PAVVEQVDLAPTLALGLGLPISQNSVGRLI 335
Cdd:cd16024  240 gelsyYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
PIGO_PIGG super family cl44747
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
743-953 4.05e-16

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: 81.86  E-value: 4.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  743 ARFVYVFVLGILFTGVKDLLRSQVMSSAVDSGRLksrgLWEVYSgvvLLVALLFRAHNLPTLacclLVQTIMAQFIwKKL 822
Cdd:pfam19316 205 ARVVFLGLALGAVYAVYRERARSRRARGGGSARL----LHELLT---LFLITQSRATNIPLF----LLFRLQLEFL-SSL 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  823 HYDAAQTTIMHYWFGQAFFYFQGNSNNIGTVDISVGFVGLESYVEAPAIILTALSTYAGPLLWACHLLCYLSSQTDRvvn 902
Cdd:pfam19316 273 DLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGYNVVAVGVLTFVSNWAGPIWWTSATNLLLLRKRRR--- 349
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688584443  903 glGHGSYCFALLRSIPAVF---YVVLV----TALRYHLFIWSVFSPKLLYE-----AMHTLIT 953
Cdd:pfam19316 350 --GEGRGVFFQHLALLTLFvaaSLVSVmaacTALRTHLFIWTVFSPKYLYTmawslGQHLLVN 410
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
66-335 1.94e-165

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: 484.76  E-value: 1.94e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  66 FKRVVIVLIDALREDFVFSSNgrRFMPYTRHVVEKGSSHSFIAKARPPTVTMPRIKALTTGSIPGFIDVVMNLNSPVLLE 145
Cdd:cd16024    4 FDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 146 DNLIWQAKSAGKRIIFYGDDTWVRLFPKHFMEQDGTTSFFVSDYTEVDNNVTRHLDSTLKRDDWDILILHYLGLDHIGHI 225
Cdd:cd16024   82 DNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 226 SGPHSSLIGPKLMEMDDIIKKIHASLisKESEGTLPNLLVVCGDHGMSETGSHGGSSEQEINTALVLISPAFRRKVGLER 305
Cdd:cd16024  162 EGPKSPLMPPKLKEMDDVIKRIYESL--EEQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPSNAD 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 688584443 306 -----PAVVEQVDLAPTLALGLGLPISQNSVGRLI 335
Cdd:cd16024  240 gelsyYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
PIGO_PIGG pfam19316
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
743-953 4.05e-16

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: 81.86  E-value: 4.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  743 ARFVYVFVLGILFTGVKDLLRSQVMSSAVDSGRLksrgLWEVYSgvvLLVALLFRAHNLPTLacclLVQTIMAQFIwKKL 822
Cdd:pfam19316 205 ARVVFLGLALGAVYAVYRERARSRRARGGGSARL----LHELLT---LFLITQSRATNIPLF----LLFRLQLEFL-SSL 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  823 HYDAAQTTIMHYWFGQAFFYFQGNSNNIGTVDISVGFVGLESYVEAPAIILTALSTYAGPLLWACHLLCYLSSQTDRvvn 902
Cdd:pfam19316 273 DLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGYNVVAVGVLTFVSNWAGPIWWTSATNLLLLRKRRR--- 349
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688584443  903 glGHGSYCFALLRSIPAVF---YVVLV----TALRYHLFIWSVFSPKLLYE-----AMHTLIT 953
Cdd:pfam19316 350 --GEGRGVFFQHLALLTLFvaaSLVSVmaacTALRTHLFIWTVFSPKYLYTmawslGQHLLVN 410
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
67-325 1.38e-14

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 76.71  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  67 KRVVIVLIDALREDFVfssnGRRFMPYTRHVVEKGSSHsfiAKARP--PTVTMPRIKALTTGS------IPGF------I 132
Cdd:COG1524   24 KKVVLILVDGLRADLL----ERAHAPNLAALAARGVYA---RPLTSvfPSTTAPAHTTLLTGLypgehgIVGNgwydpeL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 133 DVVMNLNSPVLLEDNL--------IWQ-AKSAGKR--IIF---YGDDTWVRL-FPKHFmeqDGTTSFFVSDYTevDNNVT 197
Cdd:COG1524   97 GRVVNSLSWVEDGFGSnsllpvptIFErARAAGLTtaAVFwpsFEGSGLIDAaRPYPY---DGRKPLLGNPAA--DRWIA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 198 RHLDSTLKRDDWDILILHYLGLDHIGHISGPHSSLIGPKLMEMDDIIKKIHASLiskESEGTLPN-LLVVCGDHGMSET- 275
Cdd:COG1524  172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL---KARGLYEGtLVIVTADHGMVDVp 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 276 ------------------------------------------------------------------------------GS 277
Cdd:COG1524  249 pdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGS 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 688584443 278 HGGSSEQEINTALVLISPAFRRKvglerpavVEQVDLAPTLALGLGLP 325
Cdd:COG1524  329 HGGLPDEEMRVPLLASGPGFRPG--------VRNVDVAPTIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
69-275 2.04e-09

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 60.51  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443   69 VVIVLIDALREDFVFSsngRRFMPYTRHVVEKGSShsfIAKARP--PTVTMPRIKALTTGSIPG--------FID----- 133
Cdd:pfam01663   1 LLVISLDGFRADYLDR---FELTPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  134 ----VVMNLNSPVLLEDNLIWQ-AKSAGKR--IIFYG----DDTWVRLFPKHFMEQD--GTTSFFVSDYTEVDNNVTRHL 200
Cdd:pfam01663  75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRaaALFWPgsevDYSTYYGTPPRYLKDDynNSVPFEDRVDTAVLQTWLDLP 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688584443  201 DSTLKRDDWDILILHYLGLDHIGHISGPHSSLIGPKLMEMDDIIKKIHASLisKESEGTLPNLLVVCGDHGMSET 275
Cdd:pfam01663 155 FADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPV 227
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
66-335 1.94e-165

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: 484.76  E-value: 1.94e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  66 FKRVVIVLIDALREDFVFSSNgrRFMPYTRHVVEKGSSHSFIAKARPPTVTMPRIKALTTGSIPGFIDVVMNLNSPVLLE 145
Cdd:cd16024    4 FDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSLLEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 146 DNLIWQAKSAGKRIIFYGDDTWVRLFPKHFMEQDGTTSFFVSDYTEVDNNVTRHLDSTLKRDDWDILILHYLGLDHIGHI 225
Cdd:cd16024   82 DNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHIGHL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 226 SGPHSSLIGPKLMEMDDIIKKIHASLisKESEGTLPNLLVVCGDHGMSETGSHGGSSEQEINTALVLISPAFRRKVGLER 305
Cdd:cd16024  162 EGPKSPLMPPKLKEMDDVIKRIYESL--EEQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPSNAD 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 688584443 306 -----PAVVEQVDLAPTLALGLGLPISQNSVGRLI 335
Cdd:cd16024  240 gelsyYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
66-335 3.44e-99

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: 312.96  E-value: 3.44e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  66 FKRVVIVLIDALREDFVF-------SSNGRRF---MPYTRHVVEKGSSHSFIAK--ARPPTVTMPRIKALTTGSIPGFID 133
Cdd:cd16023    4 FDKVVLLLIDALRYDFVLpddenppSENSLYYhnkLPVLEELLKSQPNNSRLFKfiADPPTTTLQRLKGLTTGSLPTFID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 134 VVMNLNSPVLLEDNLIWQAKSAGKRIIFYGDDTWVRLFPKHFMEQDGTTSFFVSDYTEVDNNVTRHLDSTLKR-DDWDIL 212
Cdd:cd16023   84 AGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSeDDWDLL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 213 ILHYLGLDHIGHISGPHSSLIGPKLMEMDDIIKKIhaslISKESEGTlpnLLVVCGDHGMSETGSHGGSSEQEINTALVL 292
Cdd:cd16023  164 IAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDI----IERLDDDT---LLLVFGDHGMTETGDHGGDSDEEVDAALFA 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688584443 293 ISPAFRRKVGLERPA----------VVEQVDLAPTLALGLGLPISQNSVGRLI 335
Cdd:cd16023  237 YSKRPFNNSDEPIESngpgdpskvrSVPQIDLVPTLSLLLGLPIPFSNLGTVI 289
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
66-335 8.56e-80

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: 261.14  E-value: 8.56e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  66 FKRVVIVLIDALREDFVFSSNGRR-FMPYTRHVVE-KGSSHSFIAKARPPTVTMPRIKALTTGSIPGFIDVVMNLNSPVL 143
Cdd:cd16019    4 YDKVVLIVIDGLRYDLAVNVNKQSsFFSFLQKLNEqPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISNFASSEI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 144 LEDNLIWQAKSAGKRIIFYGDDTWVRLFPKHFMEQDGTTSFFVSDYTEVDNNVTRHLDSTLK----RDDWDILILHYLGL 219
Cdd:cd16019   84 KEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHINDNLDeniyYDNWDFIILHFLGL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 220 DHIGHISG-PHSSLIGPKLMEMDDIIKKIhaslISKESEGTlpnLLVVCGDHGMSETGSHGGSSEQEINTALVLISP--- 295
Cdd:cd16019  164 DHLGHKHNtTSSPELEKKLDQMDNLIRDI----YDRMDNDT---LLVVVSDHGMNNDGNHGGSSTEETSSFFFFISKkgf 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 688584443 296 ----------------AFRRKVGLERPAVVEQVDLAPTLALGLGLPISQNSVGRLI 335
Cdd:cd16019  237 fkkrpidqiekikqnnEQQKIDPSEYIRIIYQIDILPTICYLLGIPIPFNNIGIII 292
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
60-334 1.43e-25

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: 108.06  E-value: 1.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  60 RAPAllfKRVVIVLIDALREDFVFSSNGRRfMPYTRHVVEK----GSSHSfiakaRPPTVTMPRIKALTTG------SI- 128
Cdd:cd16020    1 PPPA---KRLVVFVADGLRADTFFENNCSR-APFLRKIFLNqglwGISHT-----RVPTESRPGHVALFAGfyedpsAVt 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 129 ------PGFIDVVMNlNSpvllednliwqaksagKRIIFYGDDTWVRLFPK------HFMEQDGTTSFFVSDYTEVD--- 193
Cdd:cd16020   72 kgwkenPVEFDSVFN-RS----------------RRSWAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDewv 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 194 -NNVTRHLDSTLKRDDWD------ILILHYLGLDHIGHISGPHSSLIGPKLMEMDDIIKKIHASLISKESEGTLPNLLVv 266
Cdd:cd16020  135 fDKVEEFLANASSNKTELlnqdglVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFT- 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 267 cGDHGMSETGSHGGSSEQEINTALVL-----------ISPAFRRKVGLERPA--VVEQVDLAPTLALGLGLPISQNSVGR 333
Cdd:cd16020  214 -SDHGMTDWGSHGDGSPDETETPFIAwgagikhptpgRGPSFSANWGGLRLPrhDLDQADLAPLMSALLGLPPPVNSVGI 292

                 .
gi 688584443 334 L 334
Cdd:cd16020  293 L 293
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
67-323 6.09e-18

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: 84.94  E-value: 6.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  67 KRVVIVLIDALREDFVfssNGRRFMPYTRHVVEKGSShsfIAKARP--PTVTMPRIKALTTGSIP---GFIDVVM---NL 138
Cdd:cd16018    1 PPLIVISIDGFRWDYL---DRAGLTPNLKRLAEEGVR---AKYVKPvfPTLTFPNHYSIVTGLYPeshGIVGNYFydpKT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 139 NSPVLLEDNL----------IWQ-AKSAGKR--IIF--------YGDDTWVRLFPKHFMEQDGTTSFfvsdyTEVDNNVT 197
Cdd:cd16018   75 NEEFSDSDWVwdpwwiggepIWVtAEKAGLKtaSYFwpgsevaiIGYNPTPIPLGGYWQPYNDSFPF-----EERVDTIL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 198 RHLDstlkRDDWDILILHYLGLDHIGHISGPHSSLIGPKLMEMDDIIKKIHASLiskESEGTLPNL-LVVCGDHGMSETG 276
Cdd:cd16018  150 EWLD----LERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEAL---KERGLLDDTnIIVVSDHGMTDVG 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 688584443 277 SHGGS-SEQEINTALVLISPAFRRKVGLERpavVEQVDLAPTLALGLG 323
Cdd:cd16018  223 THGYDnELPDMRAIFIARGPAFKKGKKLGP---FRNVDIYPLMCNLLG 267
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
67-319 3.36e-16

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: 79.00  E-value: 3.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  67 KRVVIVLIDALREDFVF-SSNGRRFMPYTRhvVEKGSSHSFIAK-ARPPTVTMPRIKALTTGSIPGFIDVVmnlnspvll 144
Cdd:cd00016    1 KHVVLIVLDGLGADDLGkAGNPAPTTPNLK--RLASEGATFNFRsVSPPTSSAPNHAALLTGAYPTLHGYT--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 145 ednlIWQAKSAGKRIIFYGDDTWVRLFPKHFMEQDGTTSFFvsdytevdnnvtrHLDSTLKRDD---WDILILHYLGLDH 221
Cdd:cd00016   70 ----GNGSADPELPSRAAGKDEDGPTIPELLKQAGYRTGVI-------------GLLKAIDETSkekPFVLFLHFDGPDG 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 222 IGHISGPHSSLIGPKLMEMDD-IIKKIHASLISKESEGTlpnLLVVCGDHGMSETGSHG--------GSSEQEINTALVL 292
Cdd:cd00016  133 PGHAYGPNTPEYYDAVEEIDErIGKVLDALKKAGDADDT---VIIVTADHGGIDKGHGGdpkadgkaDKSHTGMRVPFIA 209
                        250       260
                 ....*....|....*....|....*..
gi 688584443 293 ISPafRRKVGLERPAVVEQVDLAPTLA 319
Cdd:cd00016  210 YGP--GVKKGGVKHELISQYDIAPTLA 234
PIGO_PIGG pfam19316
GPI ethanolamine phosphate transferase membrane region; This entry corresponds to the ...
743-953 4.05e-16

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: 81.86  E-value: 4.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  743 ARFVYVFVLGILFTGVKDLLRSQVMSSAVDSGRLksrgLWEVYSgvvLLVALLFRAHNLPTLacclLVQTIMAQFIwKKL 822
Cdd:pfam19316 205 ARVVFLGLALGAVYAVYRERARSRRARGGGSARL----LHELLT---LFLITQSRATNIPLF----LLFRLQLEFL-SSL 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  823 HYDAAQTTIMHYWFGQAFFYFQGNSNNIGTVDISVGFVGLESYVEAPAIILTALSTYAGPLLWACHLLCYLSSQTDRvvn 902
Cdd:pfam19316 273 DLSPTEITTTSLLLQYASFFAFGGSNAISSVDLSNAYNGVSGYNVVAVGVLTFVSNWAGPIWWTSATNLLLLRKRRR--- 349
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688584443  903 glGHGSYCFALLRSIPAVF---YVVLV----TALRYHLFIWSVFSPKLLYE-----AMHTLIT 953
Cdd:pfam19316 350 --GEGRGVFFQHLALLTLFvaaSLVSVmaacTALRTHLFIWTVFSPKYLYTmawslGQHLLVN 410
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
67-325 1.38e-14

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 76.71  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  67 KRVVIVLIDALREDFVfssnGRRFMPYTRHVVEKGSSHsfiAKARP--PTVTMPRIKALTTGS------IPGF------I 132
Cdd:COG1524   24 KKVVLILVDGLRADLL----ERAHAPNLAALAARGVYA---RPLTSvfPSTTAPAHTTLLTGLypgehgIVGNgwydpeL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 133 DVVMNLNSPVLLEDNL--------IWQ-AKSAGKR--IIF---YGDDTWVRL-FPKHFmeqDGTTSFFVSDYTevDNNVT 197
Cdd:COG1524   97 GRVVNSLSWVEDGFGSnsllpvptIFErARAAGLTtaAVFwpsFEGSGLIDAaRPYPY---DGRKPLLGNPAA--DRWIA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 198 RHLDSTLKRDDWDILILHYLGLDHIGHISGPHSSLIGPKLMEMDDIIKKIHASLiskESEGTLPN-LLVVCGDHGMSET- 275
Cdd:COG1524  172 AAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL---KARGLYEGtLVIVTADHGMVDVp 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 276 ------------------------------------------------------------------------------GS 277
Cdd:COG1524  249 pdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlvlvakpgwaldaplkGS 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 688584443 278 HGGSSEQEINTALVLISPAFRRKvglerpavVEQVDLAPTLALGLGLP 325
Cdd:COG1524  329 HGGLPDEEMRVPLLASGPGFRPG--------VRNVDVAPTIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
69-275 2.04e-09

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 60.51  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443   69 VVIVLIDALREDFVFSsngRRFMPYTRHVVEKGSShsfIAKARP--PTVTMPRIKALTTGSIPG--------FID----- 133
Cdd:pfam01663   1 LLVISLDGFRADYLDR---FELTPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  134 ----VVMNLNSPVLLEDNLIWQ-AKSAGKR--IIFYG----DDTWVRLFPKHFMEQD--GTTSFFVSDYTEVDNNVTRHL 200
Cdd:pfam01663  75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRaaALFWPgsevDYSTYYGTPPRYLKDDynNSVPFEDRVDTAVLQTWLDLP 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688584443  201 DSTLKRDDWDILILHYLGLDHIGHISGPHSSLIGPKLMEMDDIIKKIHASLisKESEGTLPNLLVVCGDHGMSET 275
Cdd:pfam01663 155 FADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPV 227
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
67-333 3.82e-09

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: 58.71  E-value: 3.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443  67 KRVVIVLIDALREDFV---------------FSSNGRRFmpyTRHVVekGSSHsfiakarpptvTMPRIKALTTGSIP-- 129
Cdd:cd16148    1 MNVILIVIDSLRADHLgcygydrvttpnldrLAAEGVVF---DNHYS--GSNP-----------TLPSRFSLFTGLYPfy 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 130 -GFIDVVMNLNSPVLLEdnliwQAKSAGKRIIFYGDDTWVRLFP------KHFMEQDGTTSFFVSDYTEVDNNVTRH--- 199
Cdd:cd16148   65 hGVWGGPLEPDDPTLAE-----ILRKAGYYTAAVSSNPHLFGGPgfdrgfDTFEDFRGQEGDPGEEGDERAERVTDRale 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 200 -LDSTLKRDDWdILILHYLGldhighisgPHssliGP-----KLMEMDDIIKKIHASLiskESEGTLPN-LLVVCGDHGM 272
Cdd:cd16148  140 wLDRNADDDPF-FLFLHYFD---------PH----EPylydaEVRYVDEQIGRLLDKL---KELGLLEDtLVIVTSDHGE 202
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688584443 273 S-----ETGSHGGS-SEQEINTALVLISPAFRRkvGLERPAVVEQVDLAPTLALGLGLPISQNSVGR 333
Cdd:cd16148  203 EfgehgLYWGHGSNlYDEQLHVPLIIRWPGKEP--GKRVDALVSHIDIAPTLLDLLGVEPPDYSDGR 267
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
239-325 9.51e-03

sulfatase; 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: 293746 [Multi-domain]  Cd Length: 236  Bit Score: 38.96  E-value: 9.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688584443 239 EMDDIIKKIHASLiskESEGTLPNLLVV-CGDHGMSeTGSHGGSS------EQEINTALVLISPAfRRKVGLERPAVVEQ 311
Cdd:cd16022  139 AIDDQIGRILDAL---EELGLLDNTLIVfTSDHGDM-LGDHGLRGkkgslyEGGIRVPFIVRWPG-KIPAGQVSDALVSL 213
                         90
                 ....*....|....*.
gi 688584443 312 VDLAPTL--ALGLGLP 325
Cdd:cd16022  214 LDLLPTLldLAGIEPP 229
 
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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