|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
1-407 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 765.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 1 MKRAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEAcakgeadhgRKGPLNLPNLTRLGLVKAHEGSTgkiAAGMDGNA 80
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEA---------RKGGLKLPNLAKLGLGNIATGTP---IAGVPANA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 81 EVIGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSdqeNSFPQELLDKLVKRANLPGYLGNCHSSGTVILDQLGEEH 160
Cdd:PRK05362 69 EPIGYYGKAQEVSSGKDTPTGHWEIMGVPVLFPFGYFP---NGFPQELIDEIEERAGRPGILGNKHASGTEIIDELGEEH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 161 MKTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTEGGYNIGRVIARPFVGdKAGNFQRTGNRHDLAVEPPAP 240
Cdd:PRK05362 146 MKTGKPIVYTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVG-EPGNFTRTGNRHDYALKPPAP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 241 TVLQKLvDEKNGHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAGDETIVFTNFVDFDSSWGHRRDVAGYAA 320
Cdd:PRK05362 225 TVLDKL-KEAGGEVIAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEAGDNGLVFTNLVDFDSLYGHRRDVAGYAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 321 GLELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVKPGSLGHRETFADIGQTIAKYFGTSDM 400
Cdd:PRK05362 304 ALEEFDARLPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGGSLGHRETFADIGATIADNFGVEPM 383
|
....*..
gi 1195347932 401 EYGKAMF 407
Cdd:PRK05362 384 EYGKSFL 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: 701.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 1 MKRAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEAcakgeadhgrKGPLNLPNLTRLGLVKAHEgstgkiAAGMDGNA 80
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEA----------VGGLNLPNLARLGLGNIAP------LAGLPPVE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 81 EVIGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSDqenSFPQELLDKLVKRANlPGYLGNCHSSGTVILDQLGEEH 160
Cdd:COG1015 65 EPLGAYGKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPD---GFPEELIDEFEERTG-RGVLGNKPASGTEIIEELGEEH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 161 MKTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTeGGYNIGRVIARPFVGDkAGNFQRTGNRHDLAVEPPAP 240
Cdd:COG1015 141 MRTGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLD-GEYAVGRVIARPFVGE-PGNFVRTANRHDYALKPPGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 241 TVLQKLVDeKNGHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAGdETIVFTNFVDFDSSWGHRRDVAGYAA 320
Cdd:COG1015 219 TLLDRLKE-AGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAF-GGLIFTNLVDFDSLYGHRRDVAGYAK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 321 GLELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVK-PGSLGHRETFADIGQTIAKYFGTSD 399
Cdd:COG1015 297 ALEEFDARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKpGGNLGTRETFADIGATIADHFGVPP 376
|
....*..
gi 1195347932 400 MEYGKAM 406
Cdd:COG1015 377 PGHGTSF 383
|
|
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
3-405 |
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: 658.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 3 RAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEACAKgeadhgrkgpLNLPNLTRLGLVKAHEgstgkiAAGMDGNAEV 82
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAK----------LNLPNLTKLGLGKIHE------PAGVDGNEEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 83 IGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSdqeNSFPQELLDKLVKRANLPgYLGNCHSSGTVILDQLGEEHMK 162
Cdd:TIGR01696 65 IAYYAKAHEASSGKDTMTGHWEIMGLPILFPFKVFP---NGFPQELLQKLEERAGRK-YLGNKPASGTVILDELGEEHMK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 163 TGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTEGGYNIGRVIARPFVGDkAGNFQRTGNRHDLAVEPPAPTV 242
Cdd:TIGR01696 141 TGKLIVYTSADSVLQIAAHEETFPLEELYEICEIARELTTDPKYNIGRIIARPFVGE-PGNFQRTGNRHDYALKPFAPTV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 243 LQKLVDEKNgHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAGDeTIVFTNFVDFDSSWGHRRDVAGYAAGL 322
Cdd:TIGR01696 220 LQKLKDEGH-DVISIGKIADIYDGEGITKKVRTTSNMDGMDATIKEMKEDFT-GISFTNLVDFDALWGHRRDVAGYAAAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 323 ELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVKPG-SLGHRETFADIGQTIAKYFGTSDME 401
Cdd:TIGR01696 298 ELFDRRLPELFSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGhSLGHRETFADIGATIADNFGTSDPE 377
|
....
gi 1195347932 402 YGKA 405
Cdd:TIGR01696 378 YGKS 381
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
2-406 |
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: 609.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 2 KRAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEACakgeadhgrkGPLNLPNLTRLGLVKAHEGSTGKiaagMDGNae 81
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAV----------PGLNLPNLEKLGLGNIVGIEGGP----PKEN-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 82 VIGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSdqeNSFPQELLDKLVKRANLPGyLGNCHSSGTVILDQLGEEHM 161
Cdd:cd16009 65 PIAAYGKMREASAGKDTTTGHWEIMGLKPKKPFPTFP---NGFPKELIDEFEKATGRKG-LGNKPASGTEIIKELGEEHL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 162 KTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREeLTEGGYNIGRVIARPFVGDKAGNFQRTGNRHDLAVEPPAPT 241
Cdd:cd16009 141 KTGAPIVYTSADSVFQIAAHEEVIPLEELYRICEIARE-ILDGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 242 VLQKLVdEKNGHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAgDETIVFTNFVDFDSSWGHRRDVAGYAAG 321
Cdd:cd16009 220 VLDILK-EAGIPVIGIGKIADIFAGRGITESIHTKSNADGMEKTLEALKED-FNGLIFTNLVDFDMLYGHRRDPEGYAEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 322 LELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVKPGSLGHRETFADIGQTIAKYFGTSDME 401
Cdd:cd16009 298 LEEFDRRLPELLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVNLGTRETFADIGATIADNFGVEPPE 377
|
....*
gi 1195347932 402 YGKAM 406
Cdd:cd16009 378 NGTSF 382
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
2-398 |
1.59e-86 |
|
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: 268.88 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 2 KRAFIMVLDSFGIGATEDadrfgdVGADTLGHIAEacakgeadhgrkgplnLPNLTRLglvkahegstgKIAAGMDGNAE 81
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAED------LNAKTPLHIAK----------------TPNMDKL-----------AKEYPEQLIGA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 82 VIGAYAWAHELSSGKDTpsGHWEIAGVPVLFDWGYFSDQENSFPQELLDKLVKRANLPGYLGNCHSSGTVILDQLGEEHM 161
Cdd:pfam01676 48 SGLAVGLPEGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 162 KTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTEGGYNIGRVIARPFVGDKAGNFQRTGNRHDLAVEPPAPT 241
Cdd:pfam01676 126 IEHLLALIALAKEAGAIKVHLLGDGDDRPVGYILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 242 VLQKLVDEKNGHVVSVGKIADIYANCGITKKVKA-------------------------------------------TGL 278
Cdd:pfam01676 206 LYELKLPSAGAFVPEEGKNTDGEVLEGHGLKQLRiaetekyahvtffwgggreppfpgeerylipspkvatydlqpeMSA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 279 DALFDATIKEMKEAGDetIVFTNFVDFDSSwGHRRDVAGYAAGLELFDRRLPELMELVGEDD-ILILTADHGCDPTWTGT 357
Cdd:pfam01676 286 MEITDKLLEALKEKYD--FVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDT 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1195347932 358 DHTREHIPVLVYGPKVKPGSLGH------RETFADIGQTIAKYFGTS 398
Cdd:pfam01676 363 DHTREPVPILIYGKGVRPDQVLFgekfreRGGLADIAATILMLLGLK 409
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
1-407 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 765.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 1 MKRAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEAcakgeadhgRKGPLNLPNLTRLGLVKAHEGSTgkiAAGMDGNA 80
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEA---------RKGGLKLPNLAKLGLGNIATGTP---IAGVPANA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 81 EVIGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSdqeNSFPQELLDKLVKRANLPGYLGNCHSSGTVILDQLGEEH 160
Cdd:PRK05362 69 EPIGYYGKAQEVSSGKDTPTGHWEIMGVPVLFPFGYFP---NGFPQELIDEIEERAGRPGILGNKHASGTEIIDELGEEH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 161 MKTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTEGGYNIGRVIARPFVGdKAGNFQRTGNRHDLAVEPPAP 240
Cdd:PRK05362 146 MKTGKPIVYTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVG-EPGNFTRTGNRHDYALKPPAP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 241 TVLQKLvDEKNGHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAGDETIVFTNFVDFDSSWGHRRDVAGYAA 320
Cdd:PRK05362 225 TVLDKL-KEAGGEVIAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEAGDNGLVFTNLVDFDSLYGHRRDVAGYAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 321 GLELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVKPGSLGHRETFADIGQTIAKYFGTSDM 400
Cdd:PRK05362 304 ALEEFDARLPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGGSLGHRETFADIGATIADNFGVEPM 383
|
....*..
gi 1195347932 401 EYGKAMF 407
Cdd:PRK05362 384 EYGKSFL 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: 701.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 1 MKRAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEAcakgeadhgrKGPLNLPNLTRLGLVKAHEgstgkiAAGMDGNA 80
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEA----------VGGLNLPNLARLGLGNIAP------LAGLPPVE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 81 EVIGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSDqenSFPQELLDKLVKRANlPGYLGNCHSSGTVILDQLGEEH 160
Cdd:COG1015 65 EPLGAYGKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPD---GFPEELIDEFEERTG-RGVLGNKPASGTEIIEELGEEH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 161 MKTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTeGGYNIGRVIARPFVGDkAGNFQRTGNRHDLAVEPPAP 240
Cdd:COG1015 141 MRTGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLD-GEYAVGRVIARPFVGE-PGNFVRTANRHDYALKPPGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 241 TVLQKLVDeKNGHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAGdETIVFTNFVDFDSSWGHRRDVAGYAA 320
Cdd:COG1015 219 TLLDRLKE-AGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAF-GGLIFTNLVDFDSLYGHRRDVAGYAK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 321 GLELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVK-PGSLGHRETFADIGQTIAKYFGTSD 399
Cdd:COG1015 297 ALEEFDARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKpGGNLGTRETFADIGATIADHFGVPP 376
|
....*..
gi 1195347932 400 MEYGKAM 406
Cdd:COG1015 377 PGHGTSF 383
|
|
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
3-405 |
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: 658.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 3 RAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEACAKgeadhgrkgpLNLPNLTRLGLVKAHEgstgkiAAGMDGNAEV 82
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAK----------LNLPNLTKLGLGKIHE------PAGVDGNEEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 83 IGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSdqeNSFPQELLDKLVKRANLPgYLGNCHSSGTVILDQLGEEHMK 162
Cdd:TIGR01696 65 IAYYAKAHEASSGKDTMTGHWEIMGLPILFPFKVFP---NGFPQELLQKLEERAGRK-YLGNKPASGTVILDELGEEHMK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 163 TGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTEGGYNIGRVIARPFVGDkAGNFQRTGNRHDLAVEPPAPTV 242
Cdd:TIGR01696 141 TGKLIVYTSADSVLQIAAHEETFPLEELYEICEIARELTTDPKYNIGRIIARPFVGE-PGNFQRTGNRHDYALKPFAPTV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 243 LQKLVDEKNgHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAGDeTIVFTNFVDFDSSWGHRRDVAGYAAGL 322
Cdd:TIGR01696 220 LQKLKDEGH-DVISIGKIADIYDGEGITKKVRTTSNMDGMDATIKEMKEDFT-GISFTNLVDFDALWGHRRDVAGYAAAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 323 ELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVKPG-SLGHRETFADIGQTIAKYFGTSDME 401
Cdd:TIGR01696 298 ELFDRRLPELFSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGhSLGHRETFADIGATIADNFGTSDPE 377
|
....
gi 1195347932 402 YGKA 405
Cdd:TIGR01696 378 YGKS 381
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
2-406 |
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: 609.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 2 KRAFIMVLDSFGIGATEDADRFGDVGADTLGHIAEACakgeadhgrkGPLNLPNLTRLGLVKAHEGSTGKiaagMDGNae 81
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAV----------PGLNLPNLEKLGLGNIVGIEGGP----PKEN-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 82 VIGAYAWAHELSSGKDTPSGHWEIAGVPVLFDWGYFSdqeNSFPQELLDKLVKRANLPGyLGNCHSSGTVILDQLGEEHM 161
Cdd:cd16009 65 PIAAYGKMREASAGKDTTTGHWEIMGLKPKKPFPTFP---NGFPKELIDEFEKATGRKG-LGNKPASGTEIIKELGEEHL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 162 KTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREeLTEGGYNIGRVIARPFVGDKAGNFQRTGNRHDLAVEPPAPT 241
Cdd:cd16009 141 KTGAPIVYTSADSVFQIAAHEEVIPLEELYRICEIARE-ILDGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 242 VLQKLVdEKNGHVVSVGKIADIYANCGITKKVKATGLDALFDATIKEMKEAgDETIVFTNFVDFDSSWGHRRDVAGYAAG 321
Cdd:cd16009 220 VLDILK-EAGIPVIGIGKIADIFAGRGITESIHTKSNADGMEKTLEALKED-FNGLIFTNLVDFDMLYGHRRDPEGYAEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 322 LELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPVLVYGPKVKPGSLGHRETFADIGQTIAKYFGTSDME 401
Cdd:cd16009 298 LEEFDRRLPELLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVNLGTRETFADIGATIADNFGVEPPE 377
|
....*
gi 1195347932 402 YGKAM 406
Cdd:cd16009 378 NGTSF 382
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
2-398 |
1.59e-86 |
|
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: 268.88 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 2 KRAFIMVLDSFGIGATEDadrfgdVGADTLGHIAEacakgeadhgrkgplnLPNLTRLglvkahegstgKIAAGMDGNAE 81
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAED------LNAKTPLHIAK----------------TPNMDKL-----------AKEYPEQLIGA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 82 VIGAYAWAHELSSGKDTpsGHWEIAGVPVLFDWGYFSDQENSFPQELLDKLVKRANLPGYLGNCHSSGTVILDQLGEEHM 161
Cdd:pfam01676 48 SGLAVGLPEGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 162 KTGKPIFYTSADSVFQIACHEETFGLDKLYELCEIAREELTEGGYNIGRVIARPFVGDKAGNFQRTGNRHDLAVEPPAPT 241
Cdd:pfam01676 126 IEHLLALIALAKEAGAIKVHLLGDGDDRPVGYILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 242 VLQKLVDEKNGHVVSVGKIADIYANCGITKKVKA-------------------------------------------TGL 278
Cdd:pfam01676 206 LYELKLPSAGAFVPEEGKNTDGEVLEGHGLKQLRiaetekyahvtffwgggreppfpgeerylipspkvatydlqpeMSA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 279 DALFDATIKEMKEAGDetIVFTNFVDFDSSwGHRRDVAGYAAGLELFDRRLPELMELVGEDD-ILILTADHGCDPTWTGT 357
Cdd:pfam01676 286 MEITDKLLEALKEKYD--FVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDT 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1195347932 358 DHTREHIPVLVYGPKVKPGSLGH------RETFADIGQTIAKYFGTS 398
Cdd:pfam01676 363 DHTREPVPILIYGKGVRPDQVLFgekfreRGGLADIAATILMLLGLK 409
|
|
| PRK12383 |
PRK12383 |
putative mutase; Provisional |
1-404 |
1.09e-54 |
|
putative mutase; Provisional
Pssm-ID: 237085 Cd Length: 406 Bit Score: 185.94 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 1 MKRAFIMVLDSFGIGATEDAD--RFGDVGADTLGHIAEAcakgeadhgrKGPLNLPNLTRLGLVKAHEGSTGKIAAGMDG 78
Cdd:PRK12383 1 MARFVVLVIDSFGVGAMKDVTlvRPQDAGANTCGHILSQ----------LPHLQLPTLEKLGLINALGYAPGDMQPSPSA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 79 NAeviGAYAWAHElssGKDTPSGHWEIAG----VPVLFDwgyFSDQENSFPQELLDK--------------LVKRA---- 136
Cdd:PRK12383 71 TW---GVAELQHE---GADTFMGHQEIMGtrplPPLRMP---FSDVIDRVEQALESAgyqverrgdglqflLVNQAvaig 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 137 -NLPGYLGNCHSSgTVILDQLG-EEHMKTGKpIFYTSADSVFQIACHEETFGLDKLyelceIAREELTEGGYnIGrvIAR 214
Cdd:PRK12383 142 dNLEADLGQVYNV-TANLSVISfDDALKIGR-IVREQVQVGRVIVFGGLLTDSQRI-----LDAAESKEGRF-IG--INA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 215 PfvgdKAGnFQRTGN--RH-----DLAVEppAPTVLqklvdEKNG-HVVSVGKIADIYANCGITKKVKATGLDALFDATI 286
Cdd:PRK12383 212 P----KSG-VYDNGYqvVHlgygvDPKVQ--VPQKL-----YEAGvPVVLVGKVADIVNNPYGVSWQNLVDTQRVMDITL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 287 KEMKEAGDETIvFTNFVDFDSSwGHRRDVAGYAAGLELFDRRLPELMELVGEDDILILTADHGCDPTWTGTDHTREHIPV 366
Cdd:PRK12383 280 DEFNTHPTAFI-CTNIQETDLA-GHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSHHTREVVPL 357
|
410 420 430
....*....|....*....|....*....|....*...
gi 1195347932 367 LVYGPKVKPGSLGHRETFADIGQTIAKYFGTSDMEYGK 404
Cdd:PRK12383 358 LVYQKGLQATQLGVRTTLSDVGATVCEFFGAPPPQNGR 395
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
276-377 |
2.52e-08 |
|
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: 55.17 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 276 TGLDALFDATIKEMK---------EAGDETivftnfvdfdsswGHRRDVAGYAAGLELFDRRLPELME--LVGEDDILIL 344
Cdd:cd16011 241 TDYEGKAEAALEALKdydfvfvhvKAPDEA-------------GHDGDPEAKVKAIERIDKAIVGPLLelLDGEDFVIVV 307
|
90 100 110
....*....|....*....|....*....|....
gi 1195347932 345 TADHgcdPT-WTGTDHTREHIPVLVYGPKVKPGS 377
Cdd:cd16011 308 TPDH---STpCSLKTHSGDPVPFLIYGPGVRRDG 338
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
269-392 |
6.69e-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: 53.19 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 269 ITKKVKATGLDALFDATIKEMKEAGDE--TIVFTNFVDFDSSwGH--RRDVAGYAAGLELFDRRLPELMELV-----GED 339
Cdd:cd00016 92 IPELLKQAGYRTGVIGLLKAIDETSKEkpFVLFLHFDGPDGP-GHayGPNTPEYYDAVEEIDERIGKVLDALkkagdADD 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195347932 340 DILILTADHGCDP----------TWTGTDHTREHIPVLVYGPKVKPGSLGHRET-FADIGQTIA 392
Cdd:cd00016 171 TVIIVTADHGGIDkghggdpkadGKADKSHTGMRVPFIAYGPGVKKGGVKHELIsQYDIAPTLA 234
|
|
| ApgM |
COG3635 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ... |
310-375 |
1.90e-05 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 442852 Cd Length: 398 Bit Score: 46.29 E-value: 1.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 310 GHRRDVAGYAAGLELFDRR-LPELME-LVGEDDILIL-TADHgcdPT-WTGTDHTREHIPVLVYGPKVKP 375
Cdd:COG3635 302 GHDGDLEEKVKAIERIDRRvVGPLLEgLEKFEDYRILvTPDH---PTpISLRTHSGDPVPFLIYGPGVRP 368
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
318-396 |
7.57e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 44.08 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 318 YAAGLELFDRRLPELMELVGE----DD-ILILTADHG---CDPTWTGTDH---TRE--HIPVLVYGPKVKPGslGHRETF 384
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKElgllEDtLVIVTSDHGeefGEHGLYWGHGsnlYDEqlHVPLIIRWPGKEPG--KRVDAL 242
|
90
....*....|....*
gi 1195347932 385 ---ADIGQTIAKYFG 396
Cdd:cd16148 243 vshIDIAPTLLDLLG 257
|
|
| PRK04024 |
PRK04024 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
275-375 |
1.44e-04 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235203 Cd Length: 412 Bit Score: 43.75 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 275 ATG-LDALFDATIKEMKEA-GDETIVFTNFVDFDSSwGHRRDVAGYAAGLELFDRRLPELMELVGEDDILI-LTADHGcd 351
Cdd:PRK04024 272 ATGgKDTNYMAKAKAAVELlKEYDFVLLNIKGTDEA-GHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIaVTGDHS-- 348
|
90 100
....*....|....*....|....*....
gi 1195347932 352 ptwtgT-----DHTREHIPVLVYGPKVKP 375
Cdd:PRK04024 349 -----TpvevkDHSGDPVPILIYGPGVRV 372
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
312-396 |
1.52e-04 |
|
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: 43.65 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 312 RRDVAGYAAGLELFDRRLPELMELV---GEDD--ILILTADHG-------CDPTWTGTdhtreHIPVLVYGP-KVKPGSl 378
Cdd:cd16027 185 REDLADYYDEIERLDQQVGEILDELeedGLLDntIVIFTSDHGmpfprakGTLYDSGL-----RVPLIVRWPgKIKPGS- 258
|
90 100
....*....|....*....|.
gi 1195347932 379 gHRE---TFADIGQTIAKYFG 396
Cdd:cd16027 259 -VSDalvSFIDLAPTLLDLAG 278
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
279-407 |
1.28e-03 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 40.79 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 279 DALFDATIKEMKEAGDETIVF----TNFVDFDSSWGHRR-------DVAGYAAGLELFDRRLPELMELVGEDD-----IL 342
Cdd:COG1368 369 EDLFDKALEELEKLKKPFFAFlitlSNHGPYTLPEEDKKipdygktTLNNYLNAVRYADQALGEFIEKLKKSGwydntIF 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195347932 343 ILTADHG---CDPTWTGTDHTREHIPVLVYGPKVKPGslGHRETFA---DIGQTIAKYFG---TSDMEYGKAMF 407
Cdd:COG1368 449 VIYGDHGprsPGKTDYENPLERYRVPLLIYSPGLKKP--KVIDTVGsqiDIAPTLLDLLGidyPSYYAFGRDLL 520
|
|
| apgM |
TIGR00306 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ... |
310-374 |
1.38e-03 |
|
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally characterized in archaea as 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This model describes a set of proteins in the Archaea (two each in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus) and in Aquifex aeolicus (1 member). [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273005 Cd Length: 396 Bit Score: 40.53 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1195347932 310 GHRRDVAGYAAGLELFDRRL-PELMELVGEDDILILTADHgcdPTWTGT-DHTREHIPVLVYGPKVK 374
Cdd:TIGR00306 302 GHDGDPELKVRAIEKIDSKIvGPLLALDLDETRLILTADH---STPVEVkDHSADPVPIVIVGPGVR 365
|
|
| PRK04135 |
PRK04135 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
322-382 |
1.66e-03 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 179745 [Multi-domain] Cd Length: 395 Bit Score: 40.29 E-value: 1.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1195347932 322 LELFDRRLPELMELvgEDDILILTADHGCDPTWTGtdHTREHIPVLVYGPKVKP-------------GSLGHRE 382
Cdd:PRK04135 306 IEEVDALLPEILAL--KPDVLVITGDHSTPAVLKG--HSWHPVPLLLYSKYCRPdlsqrfterecarGGLGHIP 375
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
304-377 |
1.78e-03 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 40.25 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 304 DFDSSWGHRRDVAGYAAGLELFDRRLPELMELV---GEDD--ILILTADHGcdptWTGTDHTRE-----------HIPVL 367
Cdd:COG3119 188 RDLTEEELRRARAAYAAMIEEVDDQVGRLLDALeelGLADntIVVFTSDNG----PSLGEHGLRggkgtlyeggiRVPLI 263
|
90
....*....|.
gi 1195347932 368 VYGP-KVKPGS 377
Cdd:COG3119 264 VRWPgKIKAGS 274
|
|
| IHF |
cd13832 |
Integration host factor (IHF) and similar proteins; This subfamily includes integration host ... |
260-302 |
3.17e-03 |
|
Integration host factor (IHF) and similar proteins; This subfamily includes integration host factor (IHF) and IHF-like domains. IHF is a nucleoid-associated protein (NAP) that binds and sharply bends many DNA targets in a sequence specific manner. It is a heterodimeric protein composed of two highly homologous subunits IHFA (IHF-alpha) and IHFB (IHF-beta). It is known to act as a transcription factor at many gene regulatory regions in E. coli. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups). IHF is also involved in formation as well as maintenance of bacterial biofilms since it is found in complex with extracellular DNA (eDNA) within the extracellular polymeric substances (EPS) matrix of many biofilms. This subfamily also includes the protein Hbb from tick-borne spirochete Borrelia burgdorferi, responsible for causing Lyme disease in humans. Hbb, a homodimer, shows DNA sequence preferences that are related, yet distinct from those of IHF.
Pssm-ID: 259854 Cd Length: 85 Bit Score: 36.32 E-value: 3.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1195347932 260 IADIYANCGITKKVKATGLDALFDATIKEMKEagDETIVFTNF 302
Cdd:cd13832 5 IEEIAEKTGLSKKDVKKVVDAFFDEIKEALKE--GERVELRGF 45
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
312-398 |
9.01e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 37.91 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195347932 312 RRDVAGYAAGLELFDRRLPELMELV-----GEDDILILTADHGcdptwtgtDHTREH--------------IPVLVYGPK 372
Cdd:cd16037 158 RRARAAYYGLVEFLDENIGRVLDALeelglLDNTLIIYTSDHG--------DMLGERglwgkstmyeesvrVPMIISGPG 229
|
90 100
....*....|....*....|....*....
gi 1195347932 373 VKPGslGHRETFA---DIGQTIAKYFGTS 398
Cdd:cd16037 230 IPAG--KRVKTPVslvDLAPTILEAAGAP 256
|
|
| |
