|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06078 |
PRK06078 |
pyrimidine-nucleoside phosphorylase; Reviewed |
1-433 |
0e+00 |
|
pyrimidine-nucleoside phosphorylase; Reviewed
Pssm-ID: 180387 [Multi-domain] Cd Length: 434 Bit Score: 826.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 1 MRMVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGIKVD 80
Cdd:PRK06078 1 MRMVDLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTIDLSAIEGIKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 81 KHSTGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLTPA 160
Cdd:PRK06078 81 KHSTGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFIKLVNENKVAVIGQSGNLTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 161 DKKIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISDMS 240
Cdd:PRK06078 161 DKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTVEDAEELAHAMVRIGNNVGRNTMAVISDMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 241 QPLGFAIGNALEVKEAIDTLKGEGPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQGGDS 320
Cdd:PRK06078 241 QPLGRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMVVLAGKAKTLEEAREHLIEVMNNGKALEKFKEFLSAQGGDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 321 SIVDNPEKMPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYAN 400
Cdd:PRK06078 321 SVVDDPEKLPQAKYQIEVPAKESGYISELVADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESLATIYAN 400
|
410 420 430
....*....|....*....|....*....|....
gi 2029960596 401 RENVEDVKAKIYENISIA-ETAVAPKLVHTVITD 433
Cdd:PRK06078 401 RENVEDVKAKFYKNIKISkEHVVAPELIHIIITE 434
|
|
| DeoA |
COG0213 |
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ... |
3-431 |
0e+00 |
|
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439983 [Multi-domain] Cd Length: 431 Bit Score: 794.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 3 MVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGIKVDKH 82
Cdd:COG0213 1 AVDIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSDIPGPKVDKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 83 STGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLTPADK 162
Cdd:COG0213 81 STGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAPADK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 163 KIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISDMSQP 242
Cdd:COG0213 161 KLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDMNQP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 243 LGFAIGNALEVKEAIDTLKGEGPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQGGDSSI 322
Cdd:COG0213 241 LGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGDPDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 323 VDNPEKMPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYANRE 402
Cdd:COG0213 321 VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEKGEPLATIHANDE 400
|
410 420 430
....*....|....*....|....*....|.
gi 2029960596 403 -NVEDVKAKIYENISIAETAVA-PKLVHTVI 431
Cdd:COG0213 401 aDAEEAAERLRAAYTIGDEPPEpPPLIYERI 431
|
|
| Y_phosphoryl |
TIGR02644 |
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated ... |
3-403 |
0e+00 |
|
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated pyrimidine-nucleoside phosphorylase, enzyme family EC 2.4.2.2, as in Bacillus subtilis, and more narrowly as the enzyme family EC 2.4.2.4, thymidine phosphorylase (alternate name: pyrimidine phosphorylase), as in Escherichia coli. The set of proteins encompassed by this model is designated subfamily rather than equivalog for this reason; the protein name from this model should be used when TIGR02643 does not score above trusted cutoff. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274244 [Multi-domain] Cd Length: 405 Bit Score: 654.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 3 MVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGIKVDKH 82
Cdd:TIGR02644 1 AVDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGPKVDKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 83 STGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLTPADK 162
Cdd:TIGR02644 81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 163 KIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISDMSQP 242
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 243 LGFAIGNALEVKEAIDTLKGEGPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQGGDSSI 322
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALAEDVLESGKALEKFRRFVEAQGGDPDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 323 VDNPEKMPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYANRE 402
Cdd:TIGR02644 321 IKNLDKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDPLATLYSSDP 400
|
.
gi 2029960596 403 N 403
Cdd:TIGR02644 401 I 401
|
|
| Glycos_transf_3 |
pfam00591 |
Glycosyl transferase family, a/b domain; This family includes anthranilate ... |
75-305 |
6.40e-60 |
|
Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 459860 [Multi-domain] Cd Length: 253 Bit Score: 195.58 E-value: 6.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 75 EGIKVDKHSTGGVGDTT---TLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVeGFHVEITKEQFIDIVNRDKVAVI 151
Cdd:pfam00591 1 LGDLVDIVGTGGDGDNTfniSTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 152 GQTGNLTPADKKIYALRDVTG-TVNSI--PLIAS--------SIMSKKIAAGADAIVLDVKTGAGAFMKT--EEDAKELA 218
Cdd:pfam00591 80 FAPNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGdgLDEASLLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 219 HAMVRIGNNvGRQTMAVISDMSQPLGFAIGNALEV---KEAIDTLKGE--GPEDLT--ELVLVLGSQMVVLAKKANTLEE 291
Cdd:pfam00591 160 KTTVAELKD-GEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAAhrDLVALNAGAALYLAGKADSLKE 238
|
250
....*....|....
gi 2029960596 292 AREMLIEVMKNGKA 305
Cdd:pfam00591 239 GVAKALEVIDSGKA 252
|
|
| PYNP_C |
smart00941 |
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ... |
345-418 |
1.21e-21 |
|
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as E. coli thymidine phosphorylase (TP). The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer.
Pssm-ID: 214925 [Multi-domain] Cd Length: 75 Bit Score: 87.98 E-value: 1.21e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2029960596 345 VISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYANRE-NVEDVKAKIYENISIA 418
Cdd:smart00941 1 YVTAIDARALGLAAVLLGAGRARKEDPIDYGVGIVLHKKLGDRVKKGEPLATIHANDEaELEEAAEALRAAITIS 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06078 |
PRK06078 |
pyrimidine-nucleoside phosphorylase; Reviewed |
1-433 |
0e+00 |
|
pyrimidine-nucleoside phosphorylase; Reviewed
Pssm-ID: 180387 [Multi-domain] Cd Length: 434 Bit Score: 826.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 1 MRMVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGIKVD 80
Cdd:PRK06078 1 MRMVDLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTIDLSAIEGIKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 81 KHSTGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLTPA 160
Cdd:PRK06078 81 KHSTGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFIKLVNENKVAVIGQSGNLTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 161 DKKIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISDMS 240
Cdd:PRK06078 161 DKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTVEDAEELAHAMVRIGNNVGRNTMAVISDMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 241 QPLGFAIGNALEVKEAIDTLKGEGPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQGGDS 320
Cdd:PRK06078 241 QPLGRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMVVLAGKAKTLEEAREHLIEVMNNGKALEKFKEFLSAQGGDA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 321 SIVDNPEKMPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYAN 400
Cdd:PRK06078 321 SVVDDPEKLPQAKYQIEVPAKESGYISELVADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESLATIYAN 400
|
410 420 430
....*....|....*....|....*....|....
gi 2029960596 401 RENVEDVKAKIYENISIA-ETAVAPKLVHTVITD 433
Cdd:PRK06078 401 RENVEDVKAKFYKNIKISkEHVVAPELIHIIITE 434
|
|
| DeoA |
COG0213 |
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ... |
3-431 |
0e+00 |
|
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439983 [Multi-domain] Cd Length: 431 Bit Score: 794.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 3 MVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGIKVDKH 82
Cdd:COG0213 1 AVDIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSDIPGPKVDKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 83 STGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLTPADK 162
Cdd:COG0213 81 STGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAPADK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 163 KIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISDMSQP 242
Cdd:COG0213 161 KLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDMNQP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 243 LGFAIGNALEVKEAIDTLKGEGPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQGGDSSI 322
Cdd:COG0213 241 LGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGDPDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 323 VDNPEKMPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYANRE 402
Cdd:COG0213 321 VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEKGEPLATIHANDE 400
|
410 420 430
....*....|....*....|....*....|.
gi 2029960596 403 -NVEDVKAKIYENISIAETAVA-PKLVHTVI 431
Cdd:COG0213 401 aDAEEAAERLRAAYTIGDEPPEpPPLIYERI 431
|
|
| Y_phosphoryl |
TIGR02644 |
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated ... |
3-403 |
0e+00 |
|
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated pyrimidine-nucleoside phosphorylase, enzyme family EC 2.4.2.2, as in Bacillus subtilis, and more narrowly as the enzyme family EC 2.4.2.4, thymidine phosphorylase (alternate name: pyrimidine phosphorylase), as in Escherichia coli. The set of proteins encompassed by this model is designated subfamily rather than equivalog for this reason; the protein name from this model should be used when TIGR02643 does not score above trusted cutoff. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274244 [Multi-domain] Cd Length: 405 Bit Score: 654.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 3 MVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGIKVDKH 82
Cdd:TIGR02644 1 AVDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGPKVDKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 83 STGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLTPADK 162
Cdd:TIGR02644 81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 163 KIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISDMSQP 242
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 243 LGFAIGNALEVKEAIDTLKGEGPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQGGDSSI 322
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALAEDVLESGKALEKFRRFVEAQGGDPDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 323 VDNPEKMPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYANRE 402
Cdd:TIGR02644 321 IKNLDKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDPLATLYSSDP 400
|
.
gi 2029960596 403 N 403
Cdd:TIGR02644 401 I 401
|
|
| deoA |
PRK05820 |
thymidine phosphorylase; Reviewed |
1-432 |
0e+00 |
|
thymidine phosphorylase; Reviewed
Pssm-ID: 180276 [Multi-domain] Cd Length: 440 Bit Score: 554.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 1 MRMVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIE--GIK 78
Cdd:PRK05820 2 FLAQEIIRKKRDGGALSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRDSGEVLDWSSLNlnGPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 79 VDKHSTGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLT 158
Cdd:PRK05820 82 VDKHSTGGVGDKISLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYRAFPSNDRFREILKDVGVAIIGQTSDLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 159 PADKKIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISD 238
Cdd:PRK05820 162 PADKRLYALRDVTATVESIPLITASILSKKLAEGLDALVLDVKVGSGAFMKTYEEARELARSMVEVANGAGVRTTALLTD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 239 MSQPLGFAIGNALEVKEAIDTLKGE-GPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQG 317
Cdd:PRK05820 242 MNQPLASSAGNALEVREAVEFLTGGyRPPRLVEVTMALAAEMLVLAGLAKDEAEARADLAAVLDSGKAAERFGRMVAAQG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 318 GDSSIVDNPEK-MPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVT 396
Cdd:PRK05820 322 GPPDFVENYDKyLPTAPHTKPVYADRSGVLSAMDTRALGMAVVRLGGGRRRKGDPIDYSVGLTLHARLGDRVDAGEPLAT 401
|
410 420 430
....*....|....*....|....*....|....*...
gi 2029960596 397 IYANREN-VEDVKAKIYENISIAETA-VAPKLVHTVIT 432
Cdd:PRK05820 402 LHADDEErFQEAAAALKAAIRIGDEApEATPLIYRRIT 439
|
|
| T_phosphoryl |
TIGR02643 |
thymidine phosphorylase; Thymidine phosphorylase (alternate name: pyrimidine phosphorylase), ... |
5-431 |
4.67e-141 |
|
thymidine phosphorylase; Thymidine phosphorylase (alternate name: pyrimidine phosphorylase), EC 2.4.2.4, is the designation for the enzyme of E. coli and other Proteobacteria involved in (deoxy)nucleotide degradation. It often occurs in an operon with a deoxyribose-phosphate aldolase, phosphopentomutase and a purine nucleoside phosphorylase. In many other lineages, the corresponding enzyme is designated pyrimidine-nucleoside phosphorylase (EC 2.4.2.2); the naming convention imposed by this model represents standard literature practice. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 131691 Cd Length: 437 Bit Score: 410.29 E-value: 4.67e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 5 DIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSA--IEGIKVDKH 82
Cdd:TIGR02643 5 EIIRKKRDGHSLSDAEIAQFINGITDGSVSEGQIAAFAMAVFFNGMNRDERVALTLAMRDSGDVLDWRSldLNGPVVDKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 83 STGGVGDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEGFHVEITKEQFIDIVNRDKVAVIGQTGNLTPADK 162
Cdd:TIGR02643 85 STGGVGDVVSLMLGPIVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYDIFPDPALFRRVVKDVGVAIIGQTADLAPADK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 163 KIYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAVISDMSQP 242
Cdd:TIGR02643 165 RFYATRDVTATVESIPLITASILSKKLAAGLDALVMDVKVGNGAFMPTYEESEELARSLVDVANGAGVRTTALITDMNQP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 243 LGFAIGNALEVKEAIDTLKGE-GPEDLTELVLVLGSQMVVLAKKANTLEEAREMLIEVMKNGKATEKFKEFLSNQGGDSS 321
Cdd:TIGR02643 245 LASAAGNAVEVRNAVDFLTGEkRNPRLEDVTMALAAEMLVSGGLAADEAEARAKLQAVLDSGRAAERFARMVAALGGPAD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 322 IVDNPEK-MPQAKYVIDVPAKTSGVISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYA- 399
Cdd:TIGR02643 325 FVENPERyLATAPLIKPVYADREGYVSEMDTRALGMAVVALGGGRRKADDTIDYSVGLTDLLPLGDRVEKGEPLAVVHAa 404
|
410 420 430
....*....|....*....|....*....|...
gi 2029960596 400 NRENVEDVKAKIYENISIAETAVAP-KLVHTVI 431
Cdd:TIGR02643 405 DESDAEEAAKRVKAAYRIADEAPEStPVVYRRI 437
|
|
| PRK04350 |
PRK04350 |
thymidine phosphorylase; Provisional |
4-402 |
4.74e-67 |
|
thymidine phosphorylase; Provisional
Pssm-ID: 235289 [Multi-domain] Cd Length: 490 Bit Score: 221.61 E-value: 4.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 4 VDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASA--LAMAIFfkDMTDRERADLTMAMVESGETIDLSaiEGIKVDK 81
Cdd:PRK04350 82 LSAIRKKIDGEKLDKEEIEAIIRDIVAGRYSDIELSAflTASAIN--GLDMDEIEALTRAMVETGERLDWD--RPPVVDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 82 HSTGGV-GDTTTLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVEgfHVEITKEQFIDIVNRDK-VAVIGQTGNLTP 159
Cdd:PRK04350 158 HSIGGVpGNRTTLIVVPIVAAAGLTIPKTSSRAITSPAGTADTMEVLA--PVDLSVEEIKRVVEKVGgCLVWGGAVNLSP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 160 ADKKI----YALRdvtgtVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEDAKELAHAMVRIGNNVGRQTMAV 235
Cdd:PRK04350 236 ADDILirveRPLS-----IDPRGQLVASILSKKIAAGSTHVVIDIPVGPTAKVRSVEEARRLARLFEEVGDRLGLRVECA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 236 ISDMSQPLGFAIGNALEVKEAIDTLKG--EGPEDLTELVLVLGSQMVVL---AKKANTLEEAREMLievmKNGKATEKFK 310
Cdd:PRK04350 311 ITDGSQPIGRGIGPALEARDVLAVLENdpDAPNDLREKSLRLAGILLEMggvAPGGEGYALAREIL----ESGKALEKFQ 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 311 EFLSNQGGDssivdnPEKMPQAKYVIDVPAKTSGVISNIvaDEIGIA--AMLLGAGRatkedeiDLAVGLMLRKKVGDAV 388
Cdd:PRK04350 387 EIIEAQGGD------SEDIPLGDHTHDVTAPRDGYVTAI--DNRRLAriARLAGAPK-------DKGAGIDLHVKVGDKV 451
|
410
....*....|....
gi 2029960596 389 KEGEPFVTIYANRE 402
Cdd:PRK04350 452 KKGDPLYTIHAESE 465
|
|
| Glycos_transf_3 |
pfam00591 |
Glycosyl transferase family, a/b domain; This family includes anthranilate ... |
75-305 |
6.40e-60 |
|
Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 459860 [Multi-domain] Cd Length: 253 Bit Score: 195.58 E-value: 6.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 75 EGIKVDKHSTGGVGDTT---TLVLGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVeGFHVEITKEQFIDIVNRDKVAVI 151
Cdd:pfam00591 1 LGDLVDIVGTGGDGDNTfniSTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 152 GQTGNLTPADKKIYALRDVTG-TVNSI--PLIAS--------SIMSKKIAAGADAIVLDVKTGAGAFMKT--EEDAKELA 218
Cdd:pfam00591 80 FAPNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGdgLDEASLLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 219 HAMVRIGNNvGRQTMAVISDMSQPLGFAIGNALEV---KEAIDTLKGE--GPEDLT--ELVLVLGSQMVVLAKKANTLEE 291
Cdd:pfam00591 160 KTTVAELKD-GEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAAhrDLVALNAGAALYLAGKADSLKE 238
|
250
....*....|....
gi 2029960596 292 AREMLIEVMKNGKA 305
Cdd:pfam00591 239 GVAKALEVIDSGKA 252
|
|
| PYNP_C |
pfam07831 |
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ... |
345-417 |
3.40e-25 |
|
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as E. coli thymidine phosphorylase (TP). The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer.
Pssm-ID: 429685 [Multi-domain] Cd Length: 74 Bit Score: 98.03 E-value: 3.40e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2029960596 345 VISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYANREN-VEDVKAKIYENISI 417
Cdd:pfam07831 1 YVSSIDAREIGMAAMELGAGRATKTDPIDYGVGIYLHKKLGDKVKKGEPLATIYANDEIrLEEAVKKLKKAIEI 74
|
|
| PYNP_C |
smart00941 |
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ... |
345-418 |
1.21e-21 |
|
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as E. coli thymidine phosphorylase (TP). The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer.
Pssm-ID: 214925 [Multi-domain] Cd Length: 75 Bit Score: 87.98 E-value: 1.21e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2029960596 345 VISNIVADEIGIAAMLLGAGRATKEDEIDLAVGLMLRKKVGDAVKEGEPFVTIYANRE-NVEDVKAKIYENISIA 418
Cdd:smart00941 1 YVTAIDARALGLAAVLLGAGRARKEDPIDYGVGIVLHKKLGDRVKKGEPLATIHANDEaELEEAAEALRAAITIS 75
|
|
| Glycos_trans_3N |
pfam02885 |
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ... |
4-66 |
2.01e-21 |
|
Glycosyl transferase family, helical bundle domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 460737 [Multi-domain] Cd Length: 63 Bit Score: 87.05 E-value: 2.01e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2029960596 4 VDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESG 66
Cdd:pfam02885 1 KELIKKLRDGEDLTREEARAAMDGIMSGEATDAQIAAFLMALRMKGETAEEIAGLARAMRESG 63
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
3-320 |
6.29e-08 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 54.72 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 3 MVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVE--------SGETIDLSAI 74
Cdd:PRK14607 195 IKSYLKKLVEGEDLSFEEAEDVMEDITDGNATDAQIAGFLTALRMKGETADELAGFASVMREksrhipapSPRTVDTCGT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 75 EGikvDKHSTGGVGDTTTLVlgplVAALDVPVAKMSGRGLGHTGGTIDKLEAVeGFHVEITKEQFIDivnrdkvaVIGQT 154
Cdd:PRK14607 275 GG---DGFGTFNISTTSAFV----VAAAGVPVAKHGNRAVSSKSGSADVLEAL-GVKLEMTPEEAAS--------VLRET 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 155 G-------NLTPADKKIYALRDVTGT---VNSI-PLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTEEdakelahAMVR 223
Cdd:PRK14607 339 GfsflfapLFHPAMKHAAPARRELGIrtaFNLLgPLTNPARVKYQIVGVFDPSYAEPLAQALQRLGTER-------AMVV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 224 IGNN-------VGRQTMAVISDMS--------QPLGFAIGNALEVKE---------AIDTLKGEGPEDLTELVLVLGSQM 279
Cdd:PRK14607 412 SGIDgydeistCGPTQILELEDGEivtytfdpEELGLKRVDPEELKGgdpqenyrlAEDVLKGEPRRPQRDAVALNAGAA 491
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2029960596 280 VVLAKKANTLEEAREMLIEVMKNGKATEKFKEF--LSNQGGDS 320
Cdd:PRK14607 492 LYLVGEADSIKEGVGKALDLIDDGRAYKKLEEVmdLSKTLGNS 534
|
|
| TrpD |
COG0547 |
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ... |
2-138 |
3.73e-04 |
|
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and metabolism]; Anthranilate phosphoribosyltransferase, glycosyltransferase domain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440313 [Multi-domain] Cd Length: 327 Bit Score: 42.37 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 2 RMVDIIAKKRDGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGikVDK 81
Cdd:COG0547 1 MMKELLKKLAEGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPVPLPDGDV--VDI 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029960596 82 HSTGGVGDTT----TLVlGPLVAALDVPVAKMSGRGLGHTGGTIDKLEAVeGFHVEITKEQ 138
Cdd:COG0547 79 VGTGGDGANTfnisTAA-AFVAAAAGVPVAKHGNRSVSSKSGSADVLEAL-GVNLDLSPEQ 137
|
|
| trpD |
TIGR01245 |
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, ... |
12-312 |
7.40e-03 |
|
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, Thermotoga maritima, and Archaeoglobus fulgidus, this enzymatic domain (anthranilate phosphoribosyltransferase) is found C-terminal to glutamine amidotransferase; the fusion protein is designated anthranilate synthase component II (EC 4.1.3.27) [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273522 [Multi-domain] Cd Length: 330 Bit Score: 38.40 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 12 DGKELTTEEINFFINGYTDGSIPDYQASALAMAIFFKDMTDRERADLTMAMVESGETIDLSAIEGIkVDKHSTGG----- 86
Cdd:TIGR01245 6 DGKDLSRDEAEQLMKEIMSGEASPAQIAAILTALRIKGETPEEITGFAKAMREHAVKVPGRPPEDL-VDIVGTGGdgant 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 87 --VGDTTTLVlgplVAALDVPVAKMSGRGLGHTGGTIDKLEAVeGFHVEITKEQFidivnrdkVAVIGQTG-------NL 157
Cdd:TIGR01245 85 inISTASAFV----AAAAGVKVAKHGNRSVSSKSGSADVLEAL-GVNLDLGPEKV--------ARSLEETGigflfapLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 158 TPADKKIYALRDVTG--TVNSI--PLIAssimskkiAAGADAIVLDV------KTGAGAFmkteedaKELA--HAMVRIG 225
Cdd:TIGR01245 152 HPAMKHVAPVRRELGvrTVFNLlgPLTN--------PARPKYQVIGVydpdlvEVMAEAL-------KNLGvkRALVVHG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029960596 226 NN-------VGRQTMA------VISDMSQPLGF----------AIGNALEVKEAI-DTLKGEGPEDLTELVLVLGSQMVV 281
Cdd:TIGR01245 217 DDgldeislTGPTTVAelkdgeIREYTLDPEDFglprapleelAGGSPEENAEILrDILRGKGSGAKRDIVALNAAAALY 296
|
330 340 350
....*....|....*....|....*....|.
gi 2029960596 282 LAKKANTLEEAREMLIEVMKNGKATEKFKEF 312
Cdd:TIGR01245 297 VAGRASDLKEGVELALEAIDSGAAAEKLEEL 327
|
|
| |
