|
Name |
Accession |
Description |
Interval |
E-value |
| PigN |
pfam04987 |
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a ... |
452-930 |
0e+00 |
|
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a mammalian homolog of the yeast protein MCD4P and is expressed in the endoplasmic reticulum. PIG-N is essential for glycosylphosphatidylinositol anchor synthesis. Glycosylphosphatidylinositol (GPI)-anchored proteins are cell surface-localized proteins that serve many important cellular functions.
Pssm-ID: 461508 Cd Length: 454 Bit Score: 593.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 452 EGLRYLQTYDWLFLRTIVTFGYLGWIAYALTTVIDLHVLHGTSDTDRTPASNVFFSS-----ILVALFSVFWYQSSSWRY 526
Cdd:pfam04987 1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRTTLSTLLGYKfsstlLLVLLYAFLFLQRSPLTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 527 YFYGFFPVFFWEEVFSRRKAFIAGREILLGHVSSVGdhVSFGFQSLIF-VGVLEALVHSYSYREIYTLCFILGAFWPLSY 605
Cdd:pfam04987 81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIKSSF--VKKPLIQLLLiVGVLELLVLSFFHREILSVGFVLLAFWPLFY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 606 GVEFVRKHAALSGAWAVGCLLMSVFTLLPANKVEDITTITYGAALMFLTGLLYLLFEDDIlgpshkpgavsRNGSRIIMg 685
Cdd:pfam04987 159 GTNFFRKPSLLFLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLFERSI-----------TSSSRTLL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 686 MQLGMVVLALIITRSSAASLQAKQGVPFGNQVVGWAVLVASLI-LPFAHRRYPnshyLHRLMVIFLTFAPTFIILTISYE 764
Cdd:pfam04987 227 VQVLLIALSILVTGSSVVSLQAKQGLPLGNQVVGWIILVYSLLsLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 765 GLFYFVFCMTLLGWVRLEHATYVYTAKPPATRTQETTTPLKKAStdattvvkgetyrfRTLSTSDARVALFFFFLLQSAF 844
Cdd:pfam04987 303 SLFYQAFSLELLLWIELEHELKQEESTKQSESSDTSTKKLKLSS--------------RSLTLSDLRIALFFLFFLQVAF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 845 FSTGNIASVSSFSLESVNRLNPVFNPVNQGALLILKILIPFAVISANLGILNHRLEVAPSALFMVVMAISDVMTLNFFFM 924
Cdd:pfam04987 369 FGTGNIASISSFDLDSVYRFIPVFSPFLMGALLLLKLLIPFVLVSSALGALNKRLRLPPRSLFLLVLLISDVMTLNFFFL 448
|
....*.
gi 2028200023 925 VRDEGS 930
Cdd:pfam04987 449 VRDEGS 454
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
49-366 |
4.15e-164 |
|
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: 482.86 E-value: 4.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 49 EAPAKRLVLFVADGLRADKAFElspdpdspenveggDLVHLAPFIRSRVLSHGTFGISHTRVPTESRPGHVALIAGLYED 128
Cdd:cd16020 1 PPPAKRLVVFVADGLRADTFFE--------------NNCSRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 129 VSAVATGWKLNPVNFDSVFNRSRHTWSWGSPDILPMFKEGAVPGRIDADTYSEEDeDFTSDATALDIWVFDKVKELFASA 208
Cdd:cd16020 67 PSAVTKGWKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYPEED-FDSTDASELDEWVFDKVEEFLANA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 209 KSDPelDAKLRENKIVFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEGVKEITRLVENFYGDGKTAFVFTADHGMSDWGS 288
Cdd:cd16020 146 SSNK--TELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGS 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028200023 289 HGDGHPDNTRTPLVAWGSGIstpRRPKPDAPSGHedgiSSKWNLHNVQRNDVDQADVAALMAYLVGLDFPTNSVGQLP 366
Cdd:cd16020 224 HGDGSPDETETPFIAWGAGI---KHPTPGRGPSF----SANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
45-285 |
1.46e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 79.79 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 45 DPGAEAPAKRLVLFVADGLRADKAFElspdpdspenveggdlvHLAPFIRsRVLSHGTFGISHTRV-PTESRPGHVALIA 123
Cdd:COG1524 16 AAAAAPPAKKVVLILVDGLRADLLER-----------------AHAPNLA-ALAARGVYARPLTSVfPSTTAPAHTTLLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 124 GLY--------------------------EDVSAVATGWKLNPVnFDSVFNRSRHTWSWGSPDIL-PMFKEGAVPGRIDA 176
Cdd:COG1524 78 GLYpgehgivgngwydpelgrvvnslswvEDGFGSNSLLPVPTI-FERARAAGLTTAAVFWPSFEgSGLIDAARPYPYDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 177 DTYseededFTSDATAlDIWVFDKVKELFASAKSDpeldaklrenkiVFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEG 256
Cdd:COG1524 157 RKP------LLGNPAA-DRWIAAAALELLREGRPD------------LLLVYLPDLDYAGHRYGPDSPEYRAALREVDAA 217
|
250 260
....*....|....*....|....*....
gi 2028200023 257 VKEITRLVENFYGDGKTAFVFTADHGMSD 285
Cdd:COG1524 218 LGRLLDALKARGLYEGTLVIVTADHGMVD 246
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
55-285 |
2.54e-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: 63.21 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 55 LVLFVADGLRADKAFELspdpdspenveggdlvHLAPFIrSRVLSHGTFGISHTRV-PTESRPGHVALIAGLYED----V 129
Cdd:pfam01663 1 LLVISLDGFRADYLDRF----------------ELTPNL-AALAKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGshgiV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 130 SAVATGWKLNPVNFDSVFNRSRHTWsW-GSPDILPMFKEGA------VPG-RIDADTYSEEDEDFTSDATALDIWVFDKV 201
Cdd:pfam01663 64 GNTFYDPKTGEYLVFVISDPEDPRW-WqGEPIWDTAAKAGVraaalfWPGsEVDYSTYYGTPPRYLKDDYNNSVPFEDRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 202 KELFASAK-SDPELDAKLRENKiVFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEGVKEITRLVENFYGDGKTAFVFTAD 280
Cdd:pfam01663 143 DTAVLQTWlDLPFADVAAERPD-LLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSD 221
|
....*
gi 2028200023 281 HGMSD 285
Cdd:pfam01663 222 HGMTP 226
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PigN |
pfam04987 |
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a ... |
452-930 |
0e+00 |
|
Phosphatidylinositolglycan class N (PIG-N); Phosphatidylinositolglycan class N (PIG-N) is a mammalian homolog of the yeast protein MCD4P and is expressed in the endoplasmic reticulum. PIG-N is essential for glycosylphosphatidylinositol anchor synthesis. Glycosylphosphatidylinositol (GPI)-anchored proteins are cell surface-localized proteins that serve many important cellular functions.
Pssm-ID: 461508 Cd Length: 454 Bit Score: 593.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 452 EGLRYLQTYDWLFLRTIVTFGYLGWIAYALTTVIDLHVLHGTSDTDRTPASNVFFSS-----ILVALFSVFWYQSSSWRY 526
Cdd:pfam04987 1 EGLRYYQTYDWLFLRTIVTLGYLGWIAYLLLTVLKLHVLLGSKPSSRTTLSTLLGYKfsstlLLVLLYAFLFLQRSPLTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 527 YFYGFFPVFFWEEVFSRRKAFIAGREILLGHVSSVGdhVSFGFQSLIF-VGVLEALVHSYSYREIYTLCFILGAFWPLSY 605
Cdd:pfam04987 81 YLYLLFPVYFWYQILAERPILQAGLKELFSHIKSSF--VKKPLIQLLLiVGVLELLVLSFFHREILSVGFVLLAFWPLFY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 606 GVEFVRKHAALSGAWAVGCLLMSVFTLLPANKVEDITTITYGAALMFLTGLLYLLFEDDIlgpshkpgavsRNGSRIIMg 685
Cdd:pfam04987 159 GTNFFRKPSLLFLTWLLSCLLLSVFPLLPVVKVENLPLILLGGLLILLRGLLLLLFERSI-----------TSSSRTLL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 686 MQLGMVVLALIITRSSAASLQAKQGVPFGNQVVGWAVLVASLI-LPFAHRRYPnshyLHRLMVIFLTFAPTFIILTISYE 764
Cdd:pfam04987 227 VQVLLIALSILVTGSSVVSLQAKQGLPLGNQVVGWIILVYSLLsLPLLHRTRP----LHRLLSIFLNFAPTFILLSISYE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 765 GLFYFVFCMTLLGWVRLEHATYVYTAKPPATRTQETTTPLKKAStdattvvkgetyrfRTLSTSDARVALFFFFLLQSAF 844
Cdd:pfam04987 303 SLFYQAFSLELLLWIELEHELKQEESTKQSESSDTSTKKLKLSS--------------RSLTLSDLRIALFFLFFLQVAF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 845 FSTGNIASVSSFSLESVNRLNPVFNPVNQGALLILKILIPFAVISANLGILNHRLEVAPSALFMVVMAISDVMTLNFFFM 924
Cdd:pfam04987 369 FGTGNIASISSFDLDSVYRFIPVFSPFLMGALLLLKLLIPFVLVSSALGALNKRLRLPPRSLFLLVLLISDVMTLNFFFL 448
|
....*.
gi 2028200023 925 VRDEGS 930
Cdd:pfam04987 449 VRDEGS 454
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
49-366 |
4.15e-164 |
|
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: 482.86 E-value: 4.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 49 EAPAKRLVLFVADGLRADKAFElspdpdspenveggDLVHLAPFIRSRVLSHGTFGISHTRVPTESRPGHVALIAGLYED 128
Cdd:cd16020 1 PPPAKRLVVFVADGLRADTFFE--------------NNCSRAPFLRKIFLNQGLWGISHTRVPTESRPGHVALFAGFYED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 129 VSAVATGWKLNPVNFDSVFNRSRHTWSWGSPDILPMFKEGAVPGRIDADTYSEEDeDFTSDATALDIWVFDKVKELFASA 208
Cdd:cd16020 67 PSAVTKGWKENPVEFDSVFNRSRRSWAWGSPDILPMFPKGATGGKVLTYIYPEED-FDSTDASELDEWVFDKVEEFLANA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 209 KSDPelDAKLRENKIVFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEGVKEITRLVENFYGDGKTAFVFTADHGMSDWGS 288
Cdd:cd16020 146 SSNK--TELLNQDGLVFFLHLLGLDTNGHAHKPYSKEYLENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGMTDWGS 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028200023 289 HGDGHPDNTRTPLVAWGSGIstpRRPKPDAPSGHedgiSSKWNLHNVQRNDVDQADVAALMAYLVGLDFPTNSVGQLP 366
Cdd:cd16020 224 HGDGSPDETETPFIAWGAGI---KHPTPGRGPSF----SANWGGLRLPRHDLDQADLAPLMSALLGLPPPVNSVGILP 294
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
53-352 |
6.42e-27 |
|
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: 110.20 E-value: 6.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 53 KRLVLFVADGLRADKAFElspdpdspenveGGDLVHLAPFIRSRVLSHGTFGISHTRVPTESRPGHVALIAGLYEDVSAv 132
Cdd:cd00016 1 KHVVLIVLDGLGADDLGK------------AGNPAPTTPNLKRLASEGATFNFRSVSPPTSSAPNHAALLTGAYPTLHG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 133 ATGWKLNPVNFDSVFNRsrhtWSWGSPDILPMFKE-GAVPGRIDADTYseededftsdataldiwvfdkvkelfasaksd 211
Cdd:cd00016 68 YTGNGSADPELPSRAAG----KDEDGPTIPELLKQaGYRTGVIGLLKA-------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 212 peLDAKLRENKIVFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEGVKEITRLVENFYGDGKTAFVFTADHGMSDWGSHGD 291
Cdd:cd00016 112 --IDETSKEKPFVLFLHFDGPDGPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGD 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2028200023 292 GHP--------DNTRTPLVAWGSGISTPRrpkpdapsghedgisskwnlhnVQRNDVDQADVAALMAYL 352
Cdd:cd00016 190 PKAdgkadkshTGMRVPFIAYGPGVKKGG----------------------VKHELISQYDIAPTLADL 236
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
53-363 |
8.42e-19 |
|
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: 87.62 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 53 KRLVLFVADGLRADkaFELSPDPDspenveggdlvhlAPFIRSRVLSHGTFG-ISHTRVPTESRPGHVALIAG------- 124
Cdd:cd16024 5 DKLVFMVIDALRAD--FVFGPDSN-------------MPFTQSLINSGSALAfTAKAQPPTVTMPRIKALTTGsipsfld 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 125 ---------LYED---VSAVATGWKLnpvnfdsVFnRSRHTWswgspdiLPMFkegavPGRIDAdtYSEEDEDFTSDATA 192
Cdd:cd16024 70 vvlnfasslLEEDnwlSQLKAAGKKI-------VF-YGDDTW-------LKLF-----PGSFTR--SDGTTSFFVSDFTE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 193 LDiwvfDKVkelfaSAKSDPELDaklRENKIVFFLHLLGLDTTGHGFRPYSKeyLRNIKLV--DEGVKEITRLVENFYGD 270
Cdd:cd16024 128 VD----NNV-----TRHLDSELS---RDDWDVLILHYLGLDHIGHLEGPKSP--LMPPKLKemDDVIKRIYESLEEQSSN 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 271 GKTAFVFTADHGMSDWGSHGDGHPDNTRTPLVAWGSGISTPRRPKPDAPSghedgisskwnlhnvQRNDVDQADVAALMA 350
Cdd:cd16024 194 NPTLLVVCGDHGMTDAGNHGGSSPGETSVPLLFISPKFSSKPSNADGELS---------------YYETVQQVDLAPTLA 258
|
330
....*....|...
gi 2028200023 351 YLVGLDFPTNSVG 363
Cdd:cd16024 259 LLLGLPIPKNSVG 271
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
45-285 |
1.46e-15 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 79.79 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 45 DPGAEAPAKRLVLFVADGLRADKAFElspdpdspenveggdlvHLAPFIRsRVLSHGTFGISHTRV-PTESRPGHVALIA 123
Cdd:COG1524 16 AAAAAPPAKKVVLILVDGLRADLLER-----------------AHAPNLA-ALAARGVYARPLTSVfPSTTAPAHTTLLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 124 GLY--------------------------EDVSAVATGWKLNPVnFDSVFNRSRHTWSWGSPDIL-PMFKEGAVPGRIDA 176
Cdd:COG1524 78 GLYpgehgivgngwydpelgrvvnslswvEDGFGSNSLLPVPTI-FERARAAGLTTAAVFWPSFEgSGLIDAARPYPYDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 177 DTYseededFTSDATAlDIWVFDKVKELFASAKSDpeldaklrenkiVFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEG 256
Cdd:COG1524 157 RKP------LLGNPAA-DRWIAAAALELLREGRPD------------LLLVYLPDLDYAGHRYGPDSPEYRAALREVDAA 217
|
250 260
....*....|....*....|....*....
gi 2028200023 257 VKEITRLVENFYGDGKTAFVFTADHGMSD 285
Cdd:COG1524 218 LGRLLDALKARGLYEGTLVIVTADHGMVD 246
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
53-354 |
1.42e-13 |
|
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: 71.85 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 53 KRLVLFVADGLRADkafelspDPDspenvEGGDLVHLAPFIRSRVLSHGTFGIshtrVPTESRPGHVALIAGLYEDVSAV 132
Cdd:cd16018 1 PPLIVISIDGFRWD-------YLD-----RAGLTPNLKRLAEEGVRAKYVKPV----FPTLTFPNHYSIVTGLYPESHGI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 133 ATGWKLNPvNFDSVFNRSRHTWSWGSPDILP---------------MFKEGAVPGRIDADTYSEEDEDFTS--DATALDi 195
Cdd:cd16018 65 VGNYFYDP-KTNEEFSDSDWVWDPWWIGGEPiwvtaekaglktasyFWPGSEVAIIGYNPTPIPLGGYWQPynDSFPFE- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 196 WVFDKVKELFAsaKSDPELdaklrenkivFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEGVKEITRLVENFYGDGKTAF 275
Cdd:cd16018 143 ERVDTILEWLD--LERPDL----------ILLYFEEPDSAGHKYGPDSPEVNEALKRVDRRLGYLIEALKERGLLDDTNI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 276 VFTADHGMSDWGSHG-DGHPDNTRTPLVAWGSGISTPRRPKPdapsghedgisskwnLHNVqrndvdqaDVAALMAYLVG 354
Cdd:cd16018 211 IVVSDHGMTDVGTHGyDNELPDMRAIFIARGPAFKKGKKLGP---------------FRNV--------DIYPLMCNLLG 267
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
224-363 |
3.89e-11 |
|
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: 65.07 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 224 VFFLHLLGLDTTGHGFR-PYSKEYLRNIKLVDEGVKEITRLVENfygdgKTAFVFTADHGMSDWGSHGDGHPDNTRTPLV 302
Cdd:cd16019 155 FIILHFLGLDHLGHKHNtTSSPELEKKLDQMDNLIRDIYDRMDN-----DTLLVVVSDHGMNNDGNHGGSSTEETSSFFF 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028200023 303 AWGSGISTPRRPKPDAPSGHEDGISSKwNLHNVQRNDVDQADVAALMAYLVGLDFPTNSVG 363
Cdd:cd16019 230 FISKKGFFKKRPIDQIEKIKQNNEQQK-IDPSEYIRIIYQIDILPTICYLLGIPIPFNNIG 289
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
55-285 |
2.54e-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: 63.21 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 55 LVLFVADGLRADKAFELspdpdspenveggdlvHLAPFIrSRVLSHGTFGISHTRV-PTESRPGHVALIAGLYED----V 129
Cdd:pfam01663 1 LLVISLDGFRADYLDRF----------------ELTPNL-AALAKEGVSAPNLTPVfPTLTFPNHYTLVTGLYPGshgiV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 130 SAVATGWKLNPVNFDSVFNRSRHTWsW-GSPDILPMFKEGA------VPG-RIDADTYSEEDEDFTSDATALDIWVFDKV 201
Cdd:pfam01663 64 GNTFYDPKTGEYLVFVISDPEDPRW-WqGEPIWDTAAKAGVraaalfWPGsEVDYSTYYGTPPRYLKDDYNNSVPFEDRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 202 KELFASAK-SDPELDAKLRENKiVFFLHLLGLDTTGHGFRPYSKEYLRNIKLVDEGVKEITRLVENFYGDGKTAFVFTAD 280
Cdd:pfam01663 143 DTAVLQTWlDLPFADVAAERPD-LLLVYLEEPDYAGHRYGPDSPEVEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSD 221
|
....*
gi 2028200023 281 HGMSD 285
Cdd:pfam01663 222 HGMTP 226
|
|
| GPI_EPT_3 |
cd16023 |
GPI ethanolamine phosphate transferase 3, PIG-O; Ethanolamine phosphate transferase is ... |
228-363 |
6.14e-08 |
|
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: 55.26 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 228 HLLGLDTTGHGFRPYSKEYLRNIKLVDEGVKEITRLVenfygDGKTAFVFTADHGMSDWGSHGDGHPDNTRTPLVAWGsg 307
Cdd:cd16023 166 HFLGVDHVGHRYGPNHPEMARKLTQMDQFIRDIIERL-----DDDTLLLVFGDHGMTETGDHGGDSDEEVDAALFAYS-- 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2028200023 308 istprrPKPDAPSGHEDGISSKWNLHNVQRndVDQADVAALMAYLVGLDFPTNSVG 363
Cdd:cd16023 239 ------KRPFNNSDEPIESNGPGDPSKVRS--VPQIDLVPTLSLLLGLPIPFSNLG 286
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
246-324 |
6.01e-05 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 46.26 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 246 YLRNIKLVDEGVKEITRLVENFYGDGKTAFVFTADHGMS--------DWGSHGDGHPDNTRTPLVAWGSGISTPRRPKpD 317
Cdd:pfam00884 202 YDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESlgegggylHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKS-E 280
|
....*..
gi 2028200023 318 APSGHED 324
Cdd:pfam00884 281 ALVSHVD 287
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
184-354 |
6.19e-05 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 46.14 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 184 EDFTSDATALDIW------VFDKVKELFASAKSDPeldaklrenkivFFLHLLGLDTtgHGfrPYS-------------- 243
Cdd:cd16015 123 EDFPDDEKETNGWgvsdesLFDQALEELEELKKKP------------FFIFLVTMSN--HG--PYDlpeekkdeplkvee 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 244 -----KEYLRNIKLVDEGVKE-ITRLVENFYGDgKTAFVFTADHGMS---DWGSHGDGHPDNTRTPLVAWGSGISTPRRp 314
Cdd:cd16015 187 dktelENYLNAIHYTDKALGEfIEKLKKSGLYE-NTIIVIYGDHLPSlgsDYDETDEDPLDLYRTPLLIYSPGLKKPKK- 264
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2028200023 315 kpdapsghedgisskwnlhnvQRNDVDQADVAALMAYLVG 354
Cdd:cd16015 265 ---------------------IDRVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
225-324 |
5.98e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 42.92 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028200023 225 FFLHLLGLDTtgHGfrPYskEYLRNIKLVDEGVKEITRLVENFYGDGKTAFVFTADHGMS-----DWGSHGDGHPD-NTR 298
Cdd:cd16148 150 FFLFLHYFDP--HE--PY--LYDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEfgehgLYWGHGSNLYDeQLH 223
|
90 100
....*....|....*....|....*.
gi 2028200023 299 TPLVAWGSGisTPRRPKPDAPSGHED 324
Cdd:cd16148 224 VPLIIRWPG--KEPGKRVDALVSHID 247
|
|
| |
