|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
1-406 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 722.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 1 MKRAFILVLDSFGIGETADADKFGDVGSDTMGHIADHcdqgladnadRKGPLTLPNLSKLGLAMAHKEstgRFAPGMDAD 80
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEA----------RKGGLKLPNLAKLGLGNIATG---TPIAGVPAN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 81 AEIIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTdkeNSFPKELTDRILERAGLSGFLGNCHSSGTEILDNLGEE 160
Cdd:PRK05362 68 AEPIGYYGKAQEVSSGKDTPTGHWEIMGVPVLFPFGYFP---NGFPQELIDEIEERAGRPGILGNKHASGTEIIDELGEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 161 HMKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREELED--YNIGRVIARPFIGpGKGQFERTGNRRDLSVEPPA 238
Cdd:PRK05362 145 HMKTGKPIVYTSADSVFQIAAHEEVFGLEELYRICEIAREILLDrpYNVGRVIARPFVG-EPGNFTRTGNRHDYALKPPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 239 ATILQKLaDEKGGNIHSIGKISDIYAGCGITQKTKATGIPALFEATKEAINEAGDNTIVFTNFVDFDSAYGHRRDVAGYA 318
Cdd:PRK05362 224 PTVLDKL-KEAGGEVIAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEAGDNGLVFTNLVDFDSLYGHRRDVAGYA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 319 AALEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKVPAGSLGRRDTFADIGQSLASYFGTSP 398
Cdd:PRK05362 303 AALEEFDARLPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGGSLGHRETFADIGATIADNFGVEP 382
|
....*...
gi 880813002 399 MGHGTSFL 406
Cdd:PRK05362 383 MEYGKSFL 390
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
1-406 |
0e+00 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 671.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 1 MKRAFILVLDSFGIGETADADKFGDVGSDTMGHIADHcdqgladnadrKGPLTLPNLSKLGLAMAHKestgrfAPGMDAD 80
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEA-----------VGGLNLPNLARLGLGNIAP------LAGLPPV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 81 AEIIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTDkenSFPKELTDRILERAGlSGFLGNCHSSGTEILDNLGEE 160
Cdd:COG1015 64 EEPLGAYGKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPD---GFPEELIDEFEERTG-RGVLGNKPASGTEIIEELGEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 161 HMKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREEL-EDYNIGRVIARPFIGPgKGQFERTGNRRDLSVEPPAA 239
Cdd:COG1015 140 HMRTGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLdGEYAVGRVIARPFVGE-PGNFVRTANRHDYALKPPGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 240 TILQKLADeKGGNIHSIGKISDIYAGCGITQKTKATGIPALFEATKEAINEAGdNTIVFTNFVDFDSAYGHRRDVAGYAA 319
Cdd:COG1015 219 TLLDRLKE-AGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAF-GGLIFTNLVDFDSLYGHRRDVAGYAK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 320 ALEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKVPAG-SLGRRDTFADIGQSLASYFGTSP 398
Cdd:COG1015 297 ALEEFDARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGgNLGTRETFADIGATIADHFGVPP 376
|
....*...
gi 880813002 399 MGHGTSFL 406
Cdd:COG1015 377 PGHGTSFL 384
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
2-405 |
0e+00 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 572.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 2 KRAFILVLDSFGIGETADADKFGDVGSDTMGHIADHCdqgladnadrkGPLTLPNLSKLGLAMAHKESTGrfapgmDADA 81
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAV-----------PGLNLPNLEKLGLGNIVGIEGG------PPKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 82 EIIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTdkeNSFPKELTDRILERAGLSGfLGNCHSSGTEILDNLGEEH 161
Cdd:cd16009 64 NPIAAYGKMREASAGKDTTTGHWEIMGLKPKKPFPTFP---NGFPKELIDEFEKATGRKG-LGNKPASGTEIIKELGEEH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 162 MKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREEL-EDYNIGRVIARPFIGPGKGQFERTGNRRDLSVEPPAAT 240
Cdd:cd16009 140 LKTGAPIVYTSADSVFQIAAHEEVIPLEELYRICEIAREILdGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 241 ILQKLAdEKGGNIHSIGKISDIYAGCGITQ----KTKATGIPALFEATKEAineagDNTIVFTNFVDFDSAYGHRRDVAG 316
Cdd:cd16009 220 VLDILK-EAGIPVIGIGKIADIFAGRGITEsihtKSNADGMEKTLEALKED-----FNGLIFTNLVDFDMLYGHRRDPEG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 317 YAAALEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKVPAGSLGRRDTFADIGQSLASYFGT 396
Cdd:cd16009 294 YAEALEEFDRRLPELLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVNLGTRETFADIGATIADNFGV 373
|
....*....
gi 880813002 397 SPMGHGTSF 405
Cdd:cd16009 374 EPPENGTSF 382
|
|
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
3-404 |
0e+00 |
|
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 162494 Cd Length: 381 Bit Score: 537.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 3 RAFILVLDSFGIGETADADKFGDVGSDTMGHIADHCDQgladnadrkgpLTLPNLSKLGLAMAHKestgrfAPGMDADAE 82
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAK-----------LNLPNLTKLGLGKIHE------PAGVDGNEE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 83 IIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTdkeNSFPKELTDRILERAGLSgFLGNCHSSGTEILDNLGEEHM 162
Cdd:TIGR01696 64 PIAYYAKAHEASSGKDTMTGHWEIMGLPILFPFKVFP---NGFPQELLQKLEERAGRK-YLGNKPASGTVILDELGEEHM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 163 KTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREELED--YNIGRVIARPFIGPgKGQFERTGNRRDLSVEPPAAT 240
Cdd:TIGR01696 140 KTGKLIVYTSADSVLQIAAHEETFPLEELYEICEIARELTTDpkYNIGRIIARPFVGE-PGNFQRTGNRHDYALKPFAPT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 241 ILQKLADEkGGNIHSIGKISDIYAGCGITQKTKATGIPALFEATKEAINEAGDNtIVFTNFVDFDSAYGHRRDVAGYAAA 320
Cdd:TIGR01696 219 VLQKLKDE-GHDVISIGKIADIYDGEGITKKVRTTSNMDGMDATIKEMKEDFTG-ISFTNLVDFDALWGHRRDVAGYAAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 321 LEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKV-PAGSLGRRDTFADIGQSLASYFGTSPM 399
Cdd:TIGR01696 297 LELFDRRLPELFSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVkPGHSLGHRETFADIGATIADNFGTSDP 376
|
....*
gi 880813002 400 GHGTS 404
Cdd:TIGR01696 377 EYGKS 381
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
2-398 |
3.53e-71 |
|
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 229.21 E-value: 3.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 2 KRAFILVLDSFGIGETadadkfGDVGSDTMGHIADhcdqgladnadrkgpltLPNLSKLglamahKEstgrFAPGMDADA 81
Cdd:pfam01676 1 KKVVLIVLDGWGDRPA------EDLNAKTPLHIAK-----------------TPNMDKL------AK----EYPEQLIGA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 82 EIIgAYGHAAELSSGKDTpsGHWEIAGVPVLFDWGYFTDKENSFPKELTDRILERAGLSGFLGNCHSSGTEILDNLGEEH 161
Cdd:pfam01676 48 SGL-AVGLPEGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 162 MKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREE--LEDYNIGRVIARPFIGPGKGQFERTGNRRDLSVEPPAA 239
Cdd:pfam01676 125 HIEHLLALIALAKEAGAIKVHLLGDGDDRPVGYILDGDAVitINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 240 TILQKLADEKGGNIHSIGKISDIYAGCGITQKTKA---------------------------TGIP-------------- 278
Cdd:pfam01676 205 TLYELKLPSAGAFVPEEGKNTDGEVLEGHGLKQLRiaetekyahvtffwgggreppfpgeerYLIPspkvatydlqpems 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 279 --ALFEATKEAINEAGDntIVFTNFVDFDSAyGHRRDVAGYAAALEYFDGRINEIIDMMKEDD-VLILTADHGCDPTWPG 355
Cdd:pfam01676 285 amEITDKLLEALKEKYD--FVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKD 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 880813002 356 TDHTREHIPVIVYGQKVPAGSLG------RRDTFADIGQSLASYFGTSP 398
Cdd:pfam01676 362 TDHTREPVPILIYGKGVRPDQVLfgekfrERGGLADIAATILMLLGLKK 410
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
1-406 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 722.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 1 MKRAFILVLDSFGIGETADADKFGDVGSDTMGHIADHcdqgladnadRKGPLTLPNLSKLGLAMAHKEstgRFAPGMDAD 80
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEA----------RKGGLKLPNLAKLGLGNIATG---TPIAGVPAN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 81 AEIIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTdkeNSFPKELTDRILERAGLSGFLGNCHSSGTEILDNLGEE 160
Cdd:PRK05362 68 AEPIGYYGKAQEVSSGKDTPTGHWEIMGVPVLFPFGYFP---NGFPQELIDEIEERAGRPGILGNKHASGTEIIDELGEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 161 HMKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREELED--YNIGRVIARPFIGpGKGQFERTGNRRDLSVEPPA 238
Cdd:PRK05362 145 HMKTGKPIVYTSADSVFQIAAHEEVFGLEELYRICEIAREILLDrpYNVGRVIARPFVG-EPGNFTRTGNRHDYALKPPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 239 ATILQKLaDEKGGNIHSIGKISDIYAGCGITQKTKATGIPALFEATKEAINEAGDNTIVFTNFVDFDSAYGHRRDVAGYA 318
Cdd:PRK05362 224 PTVLDKL-KEAGGEVIAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEAGDNGLVFTNLVDFDSLYGHRRDVAGYA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 319 AALEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKVPAGSLGRRDTFADIGQSLASYFGTSP 398
Cdd:PRK05362 303 AALEEFDARLPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGGSLGHRETFADIGATIADNFGVEP 382
|
....*...
gi 880813002 399 MGHGTSFL 406
Cdd:PRK05362 383 MEYGKSFL 390
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
1-406 |
0e+00 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 671.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 1 MKRAFILVLDSFGIGETADADKFGDVGSDTMGHIADHcdqgladnadrKGPLTLPNLSKLGLAMAHKestgrfAPGMDAD 80
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEA-----------VGGLNLPNLARLGLGNIAP------LAGLPPV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 81 AEIIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTDkenSFPKELTDRILERAGlSGFLGNCHSSGTEILDNLGEE 160
Cdd:COG1015 64 EEPLGAYGKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPD---GFPEELIDEFEERTG-RGVLGNKPASGTEIIEELGEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 161 HMKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREEL-EDYNIGRVIARPFIGPgKGQFERTGNRRDLSVEPPAA 239
Cdd:COG1015 140 HMRTGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLdGEYAVGRVIARPFVGE-PGNFVRTANRHDYALKPPGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 240 TILQKLADeKGGNIHSIGKISDIYAGCGITQKTKATGIPALFEATKEAINEAGdNTIVFTNFVDFDSAYGHRRDVAGYAA 319
Cdd:COG1015 219 TLLDRLKE-AGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAF-GGLIFTNLVDFDSLYGHRRDVAGYAK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 320 ALEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKVPAG-SLGRRDTFADIGQSLASYFGTSP 398
Cdd:COG1015 297 ALEEFDARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGgNLGTRETFADIGATIADHFGVPP 376
|
....*...
gi 880813002 399 MGHGTSFL 406
Cdd:COG1015 377 PGHGTSFL 384
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
2-405 |
0e+00 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 572.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 2 KRAFILVLDSFGIGETADADKFGDVGSDTMGHIADHCdqgladnadrkGPLTLPNLSKLGLAMAHKESTGrfapgmDADA 81
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAV-----------PGLNLPNLEKLGLGNIVGIEGG------PPKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 82 EIIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTdkeNSFPKELTDRILERAGLSGfLGNCHSSGTEILDNLGEEH 161
Cdd:cd16009 64 NPIAAYGKMREASAGKDTTTGHWEIMGLKPKKPFPTFP---NGFPKELIDEFEKATGRKG-LGNKPASGTEIIKELGEEH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 162 MKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREEL-EDYNIGRVIARPFIGPGKGQFERTGNRRDLSVEPPAAT 240
Cdd:cd16009 140 LKTGAPIVYTSADSVFQIAAHEEVIPLEELYRICEIAREILdGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 241 ILQKLAdEKGGNIHSIGKISDIYAGCGITQ----KTKATGIPALFEATKEAineagDNTIVFTNFVDFDSAYGHRRDVAG 316
Cdd:cd16009 220 VLDILK-EAGIPVIGIGKIADIFAGRGITEsihtKSNADGMEKTLEALKED-----FNGLIFTNLVDFDMLYGHRRDPEG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 317 YAAALEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKVPAGSLGRRDTFADIGQSLASYFGT 396
Cdd:cd16009 294 YAEALEEFDRRLPELLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVNLGTRETFADIGATIADNFGV 373
|
....*....
gi 880813002 397 SPMGHGTSF 405
Cdd:cd16009 374 EPPENGTSF 382
|
|
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
3-404 |
0e+00 |
|
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 162494 Cd Length: 381 Bit Score: 537.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 3 RAFILVLDSFGIGETADADKFGDVGSDTMGHIADHCDQgladnadrkgpLTLPNLSKLGLAMAHKestgrfAPGMDADAE 82
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAK-----------LNLPNLTKLGLGKIHE------PAGVDGNEE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 83 IIGAYGHAAELSSGKDTPSGHWEIAGVPVLFDWGYFTdkeNSFPKELTDRILERAGLSgFLGNCHSSGTEILDNLGEEHM 162
Cdd:TIGR01696 64 PIAYYAKAHEASSGKDTMTGHWEIMGLPILFPFKVFP---NGFPQELLQKLEERAGRK-YLGNKPASGTVILDELGEEHM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 163 KTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREELED--YNIGRVIARPFIGPgKGQFERTGNRRDLSVEPPAAT 240
Cdd:TIGR01696 140 KTGKLIVYTSADSVLQIAAHEETFPLEELYEICEIARELTTDpkYNIGRIIARPFVGE-PGNFQRTGNRHDYALKPFAPT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 241 ILQKLADEkGGNIHSIGKISDIYAGCGITQKTKATGIPALFEATKEAINEAGDNtIVFTNFVDFDSAYGHRRDVAGYAAA 320
Cdd:TIGR01696 219 VLQKLKDE-GHDVISIGKIADIYDGEGITKKVRTTSNMDGMDATIKEMKEDFTG-ISFTNLVDFDALWGHRRDVAGYAAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 321 LEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDHTREHIPVIVYGQKV-PAGSLGRRDTFADIGQSLASYFGTSPM 399
Cdd:TIGR01696 297 LELFDRRLPELFSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVkPGHSLGHRETFADIGATIADNFGTSDP 376
|
....*
gi 880813002 400 GHGTS 404
Cdd:TIGR01696 377 EYGKS 381
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
2-398 |
3.53e-71 |
|
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 229.21 E-value: 3.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 2 KRAFILVLDSFGIGETadadkfGDVGSDTMGHIADhcdqgladnadrkgpltLPNLSKLglamahKEstgrFAPGMDADA 81
Cdd:pfam01676 1 KKVVLIVLDGWGDRPA------EDLNAKTPLHIAK-----------------TPNMDKL------AK----EYPEQLIGA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 82 EIIgAYGHAAELSSGKDTpsGHWEIAGVPVLFDWGYFTDKENSFPKELTDRILERAGLSGFLGNCHSSGTEILDNLGEEH 161
Cdd:pfam01676 48 SGL-AVGLPEGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 162 MKTGLPIFYTSADSVFQIACHEETFGLQNLLDLCQIAREE--LEDYNIGRVIARPFIGPGKGQFERTGNRRDLSVEPPAA 239
Cdd:pfam01676 125 HIEHLLALIALAKEAGAIKVHLLGDGDDRPVGYILDGDAVitINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 240 TILQKLADEKGGNIHSIGKISDIYAGCGITQKTKA---------------------------TGIP-------------- 278
Cdd:pfam01676 205 TLYELKLPSAGAFVPEEGKNTDGEVLEGHGLKQLRiaetekyahvtffwgggreppfpgeerYLIPspkvatydlqpems 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 279 --ALFEATKEAINEAGDntIVFTNFVDFDSAyGHRRDVAGYAAALEYFDGRINEIIDMMKEDD-VLILTADHGCDPTWPG 355
Cdd:pfam01676 285 amEITDKLLEALKEKYD--FVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKD 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 880813002 356 TDHTREHIPVIVYGQKVPAGSLG------RRDTFADIGQSLASYFGTSP 398
Cdd:pfam01676 362 TDHTREPVPILIYGKGVRPDQVLfgekfrERGGLADIAATILMLLGLKK 410
|
|
| PRK12383 |
PRK12383 |
putative mutase; Provisional |
1-406 |
1.30e-48 |
|
putative mutase; Provisional
Pssm-ID: 237085 Cd Length: 406 Bit Score: 170.15 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 1 MKRAFILVLDSFGIGETADADKF--GDVGSDTMGHIADHCDQgladnadrkgpLTLPNLSKLGLAMAHKESTGRFAPGMD 78
Cdd:PRK12383 1 MARFVVLVIDSFGVGAMKDVTLVrpQDAGANTCGHILSQLPH-----------LQLPTLEKLGLINALGYAPGDMQPSPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 79 AdaeiigAYGHAAELSSGKDTPSGHWEIAG----VPVLFDwgyFTDKENSFPKELTDrileraglSGFLGNCHSSGTEIL 154
Cdd:PRK12383 70 A------TWGVAELQHEGADTFMGHQEIMGtrplPPLRMP---FSDVIDRVEQALES--------AGYQVERRGDGLQFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 155 ---------DNL----GEEHMKTGlPIFYTSADSVFQIA----CHEET-----FG-----LQNLLDlcqiAREELEDYNI 207
Cdd:PRK12383 133 lvnqavaigDNLeadlGQVYNVTA-NLSVISFDDALKIGrivrEQVQVgrvivFGglltdSQRILD----AAESKEGRFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 208 GrvIARPfigpgKGQFERTGNR-RDLSVEPPAATILQKLADEKGGNIHSIGKISDI--------YAGCGITQKtkatgip 278
Cdd:PRK12383 208 G--INAP-----KSGVYDNGYQvVHLGYGVDPKVQVPQKLYEAGVPVVLVGKVADIvnnpygvsWQNLVDTQR------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 279 aLFEATKEAINEAGDNTIvFTNFVDFDSAyGHRRDVAGYAAALEYFDGRINEIIDMMKEDDVLILTADHGCDPTWPGTDH 358
Cdd:PRK12383 274 -VMDITLDEFNTHPTAFI-CTNIQETDLA-GHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSHH 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 880813002 359 TREHIPVIVYGQKVPAGSLGRRDTFADIGQSLASYFGTSPMGHGTSFL 406
Cdd:PRK12383 351 TREVVPLLVYQKGLQATQLGVRTTLSDVGATVCEFFGAPPPQNGRSFL 398
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
268-375 |
1.17e-08 |
|
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: 55.12 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 268 ITQKTKATGIPALFEATKEAINEAGDntIVFTNFVDFDSA-YGHRRDVAGYAAALEYFDGRINEIID-----MMKEDDVL 341
Cdd:cd00016 96 LKQAGYRTGVIGLLKAIDETSKEKPF--VLFLHFDGPDGPgHAYGPNTPEYYDAVEEIDERIGKVLDalkkaGDADDTVI 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 880813002 342 ILTADHGCDP----------TWPGTDHTREHIPVIVYGQKVPAG 375
Cdd:cd00016 174 IVTADHGGIDkghggdpkadGKADKSHTGMRVPFIAYGPGVKKG 217
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
311-406 |
1.06e-07 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 53.28 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 311 RRDVAGYAAALEYFDGRINEIIDMMKEDDVL-----ILTADHG-------CDPTWPGTdhtreHIPVIVYG-QKVPAGSl 377
Cdd:cd16027 185 REDLADYYDEIERLDQQVGEILDELEEDGLLdntivIFTSDHGmpfprakGTLYDSGL-----RVPLIVRWpGKIKPGS- 258
|
90 100 110
....*....|....*....|....*....|....*
gi 880813002 378 gRRD---TFADIGQSLASYFGTSP---MgHGTSFL 406
Cdd:cd16027 259 -VSDalvSFIDLAPTLLDLAGIEPpeyL-QGRSFL 291
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
305-381 |
5.30e-07 |
|
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).
Pssm-ID: 293735 Cd Length: 368 Bit Score: 51.32 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 305 DSAyGHRRDVAGYAAALEYFDGRINEIID--MMKEDDVLILTADHgcdPT-WPGTDHTREHIPVIVYGQKVPAGSLGRRD 381
Cdd:cd16011 268 DEA-GHDGDPEAKVKAIERIDKAIVGPLLelLDGEDFVIVVTPDH---STpCSLKTHSGDPVPFLIYGPGVRRDGVTRFD 343
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
311-406 |
1.94e-05 |
|
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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 46.00 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 311 RRDVAGYAAALEYFDGRINEIIDMMKE----DDVLIL-TADHGcdptwpgtDHTREH--------------IPVIVYGQK 371
Cdd:cd16037 158 RRARAAYYGLVEFLDENIGRVLDALEElgllDNTLIIyTSDHG--------DMLGERglwgkstmyeesvrVPMIISGPG 229
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 880813002 372 VPAGslGRRDTFA---DIGQSLASYFGTSPMGH--GTSFL 406
Cdd:cd16037 230 IPAG--KRVKTPVslvDLAPTILEAAGAPPPPDldGRSLL 267
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
280-348 |
4.57e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 45.12 E-value: 4.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880813002 280 LFEATKEAInEAGDNTIVFTNFVDFDSAyGHRR--DVAGYAAALEYFDGRINEIIDMMK-----EDDVLILTADHG 348
Cdd:COG1524 170 IAAAALELL-REGRPDLLLVYLPDLDYA-GHRYgpDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTADHG 243
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
317-406 |
1.25e-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: 43.31 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 317 YAAALEYFDGRINEIIDMMKE----DD-VLILTADHG---------CDPTWPGTDHTReHIPVIVYGQKVPAGslGRRDT 382
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKElgllEDtLVIVTSDHGeefgehglyWGHGSNLYDEQL-HVPLIIRWPGKEPG--KRVDA 241
|
90 100
....*....|....*....|....*....
gi 880813002 383 F---ADIGQSLASYFGTSPMG--HGTSFL 406
Cdd:cd16148 242 LvshIDIAPTLLDLLGVEPPDysDGRSLL 270
|
|
| PRK04024 |
PRK04024 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
285-372 |
2.49e-04 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235203 Cd Length: 412 Bit Score: 42.98 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 285 KEAINEAGDNTIVFTNFVDFDSAyGHRRDVAGYAAALEYFDGRINEIIDMMKEDDVLI-LTADHgcdpTWPGT--DHTRE 361
Cdd:PRK04024 285 KAAVELLKEYDFVLLNIKGTDEA-GHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIaVTGDH----STPVEvkDHSGD 359
|
90
....*....|.
gi 880813002 362 HIPVIVYGQKV 372
Cdd:PRK04024 360 PVPILIYGPGV 370
|
|
| ALP |
cd16012 |
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ... |
273-369 |
2.14e-03 |
|
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound 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. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.
Pssm-ID: 293736 Cd Length: 283 Bit Score: 39.72 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880813002 273 KATGIPALFEATKEAIN-------------EAGDntIvftnfvdfDSAyGHRRDVAGYAAALEYFDGRINEIIDMMKEDD 339
Cdd:cd16012 166 DETDEPSLAEMTEKAIEvlsknpkgfflmvEGGR--I--------DWA-GHANDAARAIEETLAFDKAVKVALDFAKKDG 234
|
90 100 110
....*....|....*....|....*....|..
gi 880813002 340 --VLILTADHgcdptwpGTDHTREHIPVIVYG 369
Cdd:cd16012 235 dtLVIVTADH-------ETGHTGEDVPVFAYG 259
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
301-348 |
3.24e-03 |
|
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: 39.11 E-value: 3.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 880813002 301 FVDFDSAyGHR--RDVAGYAAALEYFDGRINEIIDMMKE----DDV-LILTADHG 348
Cdd:cd16018 164 FEEPDSA-GHKygPDSPEVNEALKRVDRRLGYLIEALKErgllDDTnIIVVSDHG 217
|
|
| |
