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Conserved domains on  [gi|1067605065|ref|NP_001332918|]
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GPI ethanolamine phosphate transferase 2 isoform 10 [Homo sapiens]

Protein Classification

GPI ethanolamine phosphate transferase 2( domain architecture ID 10888022)

GPI (glycosylphosphatidylinositol) ethanolamine phosphate transferase 2 catalyzes the transfer of ethanolamine phosphate to the second mannose of the GPI-anchor

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 1.79e-167

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: 477.83  E-value: 1.79e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  62 PPLFSKVVIVLIDALRDDFVFGSKgvKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPA 141
Cdd:cd16024     1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 142 LLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHI 221
Cdd:cd16024    79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 222 GHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP- 300
Cdd:cd16024   159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1067605065 301 ---GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 335
Cdd:cd16024   237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 62-335 1.79e-167

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: 477.83  E-value: 1.79e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  62 PPLFSKVVIVLIDALRDDFVFGSKgvKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPA 141
Cdd:cd16024     1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 142 LLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHI 221
Cdd:cd16024    79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 222 GHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP- 300
Cdd:cd16024   159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1067605065 301 ---GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 335
Cdd:cd16024   237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 49-325 2.38e-16

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 80.95  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  49 PSAGASSNWTTLPPPlfsKVVIVLIDALRDDFVfgskGVKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGS 126
Cdd:COG1524    10 ASLLAAAAAAAPPAK---KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 127 LPG----------FVDVIRNLNSPALLED-----------SVIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DG 179
Cdd:COG1524    80 YPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpTIFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 180 TTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPL 259
Cdd:COG1524   157 RKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 260 PNLLVLCGDHGMSET----------------------------------------------------------------- 274
Cdd:COG1524   233 GTLVIVTADHGMVDVppdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlv 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067605065 275 --------------GSHGASSTEEVNTPLILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 325
Cdd:COG1524   313 lvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF---------RPGVRNVDVAPTIARLLGLP 368
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 68-279 1.71e-10

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


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 62.82  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  68 VVIVLIDALRDDFVFGSKGvkfMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD----- 132
Cdd:pfam01663   1 LLVISLDGFRADYLDRFEL---TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 133 ----VIRNLNSPALLEDSVIRQ-AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR--- 197
Cdd:pfam01663  75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwl 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 198 -HLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSETGS 276
Cdd:pfam01663 152 dLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSD 229


                  ...
gi 1067605065 277 HGA 279
Cdd:pfam01663 230 DKV 232
 
Name Accession Description Interval E-value
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 62-335 1.79e-167

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: 477.83  E-value: 1.79e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  62 PPLFSKVVIVLIDALRDDFVFGSKgvKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPA 141
Cdd:cd16024     1 KPAFDKLVFMVIDALRADFVFGPD--SNMPFTQSLINSGSALAFTAKAQPPTVTMPRIKALTTGSIPSFLDVVLNFASSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 142 LLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHI 221
Cdd:cd16024    79 LEEDNWLSQLKAAGKKIVFYGDDTWLKLFPGSFTRSDGTTSFFVSDFTEVDNNVTRHLDSELSRDDWDVLILHYLGLDHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 222 GHISGPNSPLIGQKLSEMDSVLMKIHTSLQskERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP- 300
Cdd:cd16024   159 GHLEGPKSPLMPPKLKEMDDVIKRIYESLE--EQSSNNPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPs 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1067605065 301 ---GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLL 335
Cdd:cd16024   237 nadGELSYYETVQQVDLAPTLALLLGLPIPKNSVGVLI 274
GPI_EPT_3 cd16023
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ...
 62-334 1.21e-98

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: 302.56  E-value: 1.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  62 PPLFSKVVIVLIDALRDDFVF-------GSKGVKF---MPYTTYLVEKGASHS----FVAEakPPTVTMPRIKALMTGSL 127
Cdd:cd16023     1 PPRFDKVVLLLIDALRYDFVLpddenppSENSLYYhnkLPVLEELLKSQPNNSrlfkFIAD--PPTTTLQRLKGLTTGSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 128 PGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRG- 206
Cdd:cd16023    79 PTFIDAGSNFASSAIVEDNLLKQLKLAGKRIVFMGDDTWTSLFPNQFDRSYPFPSFNVKDLDTVDNGVLKHLFPELQSEd 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 207 DWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKereTplpnLLVLCGDHGMSETGSHGASSTEEVN 286
Cdd:cd16023   159 DWDLLIAHFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERLDDD---T----LLLVFGDHGMTETGDHGGDSDEEVD 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1067605065 287 TPLILIS---------SAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSL 334
Cdd:cd16023   232 AALFAYSkrpfnnsdePIESNGPGDPSKVRSVPQIDLVPTLSLLLGLPIPFSNLGTV 288
GPI_EPT cd16019
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ...
 62-332 2.63e-76

GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293743 [Multi-domain]  Cd Length: 292  Bit Score: 244.58  E-value: 2.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  62 PPLFSKVVIVLIDALRDDFVF--GSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNS 139
Cdd:cd16019     1 PTKYDKVVLIVIDGLRYDLAVnvNKQSSFFSFLQKLNEQPNNSFLALSFADPPTVTGPRLKALTTGNPPTFLDLISNFAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 140 PALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHL----DKVLKRGDWDILILHY 215
Cdd:cd16019    81 SEIKEDNIIRQLKKNGKKILFYGDDTWLDLFPEIFTYKFTITSFNIRDMHDVDPIFYNHIndnlDENIYYDNWDFIILHF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 216 LGLDHIGHISG-PNSPLIGQKLSEMDSVLMKIHTSLQSKeretplpNLLVLCGDHGMSETGSHGASSTEEVNTPLILIS- 293
Cdd:cd16019   161 LGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDND-------TLLVVVSDHGMNNDGNHGGSSTEETSSFFFFISk 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1067605065 294 SAFERKPGDIRHPKHVQ-----------------QTDVAATLAIALGLPIPKDSVG 332
Cdd:cd16019   234 KGFFKKRPIDQIEKIKQnneqqkidpseyiriiyQIDILPTICYLLGIPIPFNNIG 289
GPI_EPT_1 cd16020
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ...
 62-334 1.83e-23

GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293744  Cd Length: 294  Bit Score: 100.74  E-value: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  62 PPLFSKVVIVLIDALRDDFVFGSKgvkfMPYTTYL----VEKGA---SHSFVaeakpPTVTMPRIKALMTGSlpgFVD-- 132
Cdd:cd16020     1 PPPAKRLVVFVADGLRADTFFENN----CSRAPFLrkifLNQGLwgiSHTRV-----PTESRPGHVALFAGF---YEDps 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 133 -VIRNLNSPALLEDSVIRQAKAAgkriVFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKR 205
Cdd:cd16020    69 aVTKGWKENPVEFDSVFNRSRRS----WAWGSPDILPMFPKgatggkVLTYIYPEEDFDSTDASELDEWVFDKVEEFLAN 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 206 GDWD----------ILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQS--KERETPLpnllVLCGDHGMSE 273
Cdd:cd16020   145 ASSNktellnqdglVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEyfNDGRTAY----IFTSDHGMTD 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067605065 274 TGSHGASSTEEVNTPLIL-----------ISSAFERKPGDIRHPKH-VQQTDVAATLAIALGLPIPKDSVGSL 334
Cdd:cd16020   221 WGSHGDGSPDETETPFIAwgagikhptpgRGPSFSANWGGLRLPRHdLDQADLAPLMSALLGLPPPVNSVGIL 293
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 66-323 7.10e-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: 81.09  E-value: 7.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  66 SKVVIVLIDALRDDFVfgSKGvKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLP---GFVD---VIRNL 137
Cdd:cd16018     1 PPLIVISIDGFRWDYL--DRA-GLTPNLKRLAEEGVR---AKYVKPvfPTLTFPNHYSIVTGLYPeshGIVGnyfYDPKT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 138 NSPALLEDSV-----IR------QAKAAGKRIVFYgdeTWvklfPKHFVEYDGT--TSFFVSDYTEVDNNVTRHLDKV-- 202
Cdd:cd16018    75 NEEFSDSDWVwdpwwIGgepiwvTAEKAGLKTASY---FW----PGSEVAIIGYnpTPIPLGGYWQPYNDSFPFEERVdt 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 203 ----LKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLpNLLVLcGDHGMSETGSHG 278
Cdd:cd16018   148 ilewLDLERPDLILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDT-NIIVV-SDHGMTDVGTHG 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1067605065 279 ASSTE-EVNTPLILissafeRKPgDIRHPKHV---QQTDVAATLAIALG 323
Cdd:cd16018   226 YDNELpDMRAIFIA------RGP-AFKKGKKLgpfRNVDIYPLMCNLLG 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 49-325 2.38e-16

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 80.95  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  49 PSAGASSNWTTLPPPlfsKVVIVLIDALRDDFVfgskGVKFMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGS 126
Cdd:COG1524    10 ASLLAAAAAAAPPAK---KVVLILVDGLRADLL----ERAHAPNLAALAARGVY---ARPLTSvfPSTTAPAHTTLLTGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 127 LPG----------FVDVIRNLNSPALLED-----------SVIRQAKAAGKRIVFYGdetWVKLFPKHFVEY------DG 179
Cdd:COG1524    80 YPGehgivgngwyDPELGRVVNSLSWVEDgfgsnsllpvpTIFERARAAGLTTAAVF---WPSFEGSGLIDAarpypyDG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 180 TTSFFVSDYTevDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPL 259
Cdd:COG1524   157 RKPLLGNPAA--DRWIAAAALELLREGRPDLLLVYLPDLDYAGHRYGPDSPEYRAALREVDAALGRLLDAL--KARGLYE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 260 PNLLVLCGDHGMSET----------------------------------------------------------------- 274
Cdd:COG1524   233 GTLVIVTADHGMVDVppdidlnrlrlagllavragesahlylkdgadaevrallglparvltreelaaghfgphrigdlv 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067605065 275 --------------GSHGASSTEEVNTPLILISSAFerkpgdirhPKHVQQTDVAATLAIALGLP 325
Cdd:COG1524   313 lvakpgwaldaplkGSHGGLPDEEMRVPLLASGPGF---------RPGVRNVDVAPTIARLLGLP 368
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 68-319 3.45e-14

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 72.45  E-value: 3.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  68 VVIVLIDALRDDFVFgsKGVKFMPYTTYLvEKGASHSFVAEAK---PPTVTMPRIKALMTGSLPGFVDVIRNL------- 137
Cdd:cd00016     3 VVLIVLDGLGADDLG--KAGNPAPTTPNL-KRLASEGATFNFRsvsPPTSSAPNHAALLTGAYPTLHGYTGNGsadpelp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 138 ---NSPALLEDSVIRQAKAAGKRIVFYGdetwvklFPKHFVEydgttsffvsdytevdnnvtrhldkvLKRGDWDILILH 214
Cdd:cd00016    80 sraAGKDEDGPTIPELLKQAGYRTGVIG-------LLKAIDE--------------------------TSKEKPFVLFLH 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 215 YLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSK--ERETplpnLLVLCGDHGMSETGSHGA--------SSTEE 284
Cdd:cd00016   127 FDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAgdADDT----VIIVTADHGGIDKGHGGDpkadgkadKSHTG 202

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1067605065 285 VNTPLILISSAFeRKPGDIRHPkhVQQTDVAATLA 319
Cdd:cd00016   203 MRVPFIAYGPGV-KKGGVKHEL--ISQYDIAPTLA 234
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 68-279 1.71e-10

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


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 62.82  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  68 VVIVLIDALRDDFVFGSKGvkfMPYTTYLVEKGAShsfVAEAKP--PTVTMPRIKALMTGSLPG--------FVD----- 132
Cdd:pfam01663   1 LLVISLDGFRADYLDRFEL---TPNLAALAKEGVS---APNLTPvfPTLTFPNHYTLVTGLYPGshgivgntFYDpktge 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 133 ----VIRNLNSPALLEDSVIRQ-AKAAGKRIVFYGdetWVKLFPKHFVEYDGTTSFFVSDYT-------EVDNNVTR--- 197
Cdd:pfam01663  75 ylvfVISDPEDPRWWQGEPIWDtAAKAGVRAAALF---WPGSEVDYSTYYGTPPRYLKDDYNnsvpfedRVDTAVLQtwl 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 198 -HLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLqsKERETPLPNLLVLCGDHGMSETGS 276
Cdd:pfam01663 152 dLPFADVAAERPDLLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEAL--DERGLFEDTNVIVVSDHGMTPVSD 229


                  ...
gi 1067605065 277 HGA 279
Cdd:pfam01663 230 DKV 232
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 67-337 1.41e-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: 59.10  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065  67 KVVIVLIDALRDDFV--FGSKGVKfMPYTTYLVEKGA------SHSfvaeakPPTvtMPRIKALMTGSLPGFVDVIRNLN 138
Cdd:cd16148     2 NVILIVIDSLRADHLgcYGYDRVT-TPNLDRLAAEGVvfdnhySGS------NPT--LPSRFSLFTGLYPFYHGVWGGPL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 139 SPALleDSVIRQAKAAGKRIVFYGDETWVKLFPK------HFVEYDGTTSFFVSDYTEVDNNVTRH----LDKVLKRGDW 208
Cdd:cd16148    73 EPDD--PTLAEILRKAGYYTAAVSSNPHLFGGPGfdrgfdTFEDFRGQEGDPGEEGDERAERVTDRalewLDRNADDDPF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 209 dILILHYLGldhighisgPNSP-LIGQKLSEMDSVLMKIHTSLQSKER--ETplpnLLVLCGDHGMS-----ETGSHGAS 280
Cdd:cd16148   151 -FLFLHYFD---------PHEPyLYDAEVRYVDEQIGRLLDKLKELGLleDT----LVIVTSDHGEEfgehgLYWGHGSN 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1067605065 281 STEE-VNTPLILissAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFP 337
Cdd:cd16148   217 LYDEqLHVPLII---RWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 262-326 5.64e-04

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: 42.36  E-value: 5.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 262 LLVLCGDHGmSETGSHGASST-----EEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPI 326
Cdd:cd16153   201 IVYVTGDHG-WHLGEQGILAKftfwpQSHRVPLIVVSSDKLKAPAGKVRHDFVEFVDLAPTLLAAAGVDV 269
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
262-343 6.42e-04

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 42.56  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 262 LLVLCGDHGMSeTGSHG-----ASSTEE-VNTPLIlISSAFERKPGDIRHpKHVQQTDVAATLAIALGLPIPKDSVG-SL 334
Cdd:COG3119   230 IVVFTSDNGPS-LGEHGlrggkGTLYEGgIRVPLI-VRWPGKIKAGSVSD-ALVSLIDLLPTLLDLAGVPIPEDLDGrSL 306


                  ....*....
gi 1067605065 335 LfPVVEGRP 343
Cdd:COG3119   307 L-PLLTGEK 314
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 259-346 9.39e-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: 41.98  E-value: 9.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 259 LPNLLVL-CGDHGMSeTGSH-----GASSTEEV-NTPLILISSAFERKPGDIRHPkhVQQTDVAATLAIALGLPIPKDSV 331
Cdd:cd16156   265 AEDAWVIyTSDHGDM-LGAHklwakGPAVYDEItNIPLIIRGKGGEKAGTVTDTP--VSHIDLAPTILDYAGIPQPKVLE 341

                          90
                  ....*....|....*
gi 1067605065 332 GSLLFPVVEGRPMRE 346
Cdd:cd16156   342 GESILATIEDPEIPE 356
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 262-357 4.01e-03

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 39.86  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067605065 262 LLVLCGDHGMSeTGSHG---ASSTEE--VNTPLILISsaferkPG-----DIRHPkhVQQTDVAATLAIALGLPIPKDSV 331
Cdd:cd16155   222 IIVFTSDHGLA-VGSHGlmgKQNLYEhsMRVPLIISG------PGipkgkRRDAL--VYLQDVFPTLCELAGIEIPESVE 292

                          90       100
                  ....*....|....*....|....*...
gi 1067605065 332 GSLLFPVVEG--RPMREQLrFLHLNTVQ 357
Cdd:cd16155   293 GKSLLPVIRGekKAVRDTL-YGAYRDGQ 319
 
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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