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Conserved domains on  [gi|4503445|ref|NP_001944|]
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thymidine phosphorylase isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DeoA super family cl43065
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
 38-470 0e+00

Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


The actual alignment was detected with superfamily member COG0213:

Pssm-ID: 439983 [Multi-domain]  Cd Length: 431  Bit Score: 520.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrqqL----V 113
Cdd:COG0213   3 DIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSD-----IpgpkV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  114 DKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVP 193
Cdd:COG0213  78 DKHSTGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAP 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  194 ADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAM 273
Cdd:COG0213 158 ADKKLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDM 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  274 DKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVD 353
Cdd:COG0213 238 NQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGD 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  354 PGLaralcsgspAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRR 433
Cdd:COG0213 318 PDV---------VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEK 388

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503445  434 GTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAP 470
Cdd:COG0213 389 GEPLATIHANDEADAEEAAERLRAAYTIGDEPPEPPP 425
 
Name Accession Description Interval E-value
DeoA COG0213
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
 38-470 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: 520.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrqqL----V 113
Cdd:COG0213   3 DIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSD-----IpgpkV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  114 DKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVP 193
Cdd:COG0213  78 DKHSTGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAP 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  194 ADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAM 273
Cdd:COG0213 158 ADKKLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDM 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  274 DKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVD 353
Cdd:COG0213 238 NQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGD 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  354 PGLaralcsgspAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRR 433
Cdd:COG0213 318 PDV---------VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEK 388

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503445  434 GTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAP 470
Cdd:COG0213 389 GEPLATIHANDEADAEEAAERLRAAYTIGDEPPEPPP 425
Y_phosphoryl TIGR02644
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated ...
 37-446 5.78e-159

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: 456.31  E-value: 5.78e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445     37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQqLVDKH 116
Cdd:TIGR02644   2 VDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGP-KVDKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    117 STGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADG 196
Cdd:TIGR02644  81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    197 ILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKP 276
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    277 LGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGL 356
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALAEDVLESGKALEKFRRFVEAQGGDPDV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    357 ARALcsgspaerrQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTP 436
Cdd:TIGR02644 321 IKNL---------DKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDP 391

                         410
                  ....*....|
gi 4503445    437 WLRVHRDGPA 446
Cdd:TIGR02644 392 LATLYSSDPI 401
deoA PRK05820
thymidine phosphorylase; Reviewed
 37-470 7.69e-159

thymidine phosphorylase; Reviewed


Pssm-ID: 180276 [Multi-domain]  Cd Length: 440  Bit Score: 457.37  E-value: 7.69e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQ-LVDK 115
Cdd:PRK05820   5 QEIIRKKRDGGALSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRDSGEVLDWSSLNLNGpIVDK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   116 HSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPAD 195
Cdd:PRK05820  85 HSTGGVGDKISLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYRAFPSNDRFREILKDVGVAIIGQTSDLAPAD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   196 GILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDK 275
Cdd:PRK05820 165 KRLYALRDVTATVESIPLITASILSKKLAEGLDALVLDVKVGSGAFMKTYEEARELARSMVEVANGAGVRTTALLTDMNQ 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   276 PLGRCVGHALEVEEALLCMDGA-GPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDP 354
Cdd:PRK05820 245 PLASSAGNALEVREAVEFLTGGyRPPRLVEVTMALAAEMLVLAGLAKDEAEARADLAAVLDSGKAAERFGRMVAAQGGPP 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   355 GLARALCSGspaerrqlLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRG 434
Cdd:PRK05820 325 DFVENYDKY--------LPTAPHTKPVYADRSGVLSAMDTRALGMAVVRLGGGRRRKGDPIDYSVGLTLHARLGDRVDAG 396

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 4503445   435 TPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAP 470
Cdd:PRK05820 397 EPLATLHADDEERFQEAAAALKAAIRIGDEAPEATP 432
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
 109-340 3.86e-65

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: 210.61  E-value: 3.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    109 RQQLVDKHSTGGVGDK---VSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCCIV 185
Cdd:pfam00591   1 LGDLVDIVGTGGDGDNtfnISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    186 GQSEQLVPADGILYAARDVTA-TVDSL--PLITA--------SILSKKLVEGLSALVVDVKFGGAAVFPN--QEQARELA 252
Cdd:pfam00591  80 FAPNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGdgLDEASLLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    253 KTLVGVGAsLGLRVAAALTAMDKPLGRCVGHALEV---EEALLCMDGA--GPPDL--RDLVTTLGGALLWLSGHAGTQAQ 325
Cdd:pfam00591 160 KTTVAELK-DGEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAahRDLVALNAGAALYLAGKADSLKE 238

                         250
                  ....*....|....*
gi 4503445    326 GAARVAAALDDGSAL 340
Cdd:pfam00591 239 GVAKALEVIDSGKAL 253
PYNP_C smart00941
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
 389-462 1.16e-13

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: 66.02  E-value: 1.16e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503445     389 VELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLS 462
Cdd:smart00941   2 VTAIDARALGLAAVLLGAGRARKEDPIDYGVGIVLHKKLGDRVKKGEPLATIHANDEAELEEAAEALRAAITIS 75
 
Name Accession Description Interval E-value
DeoA COG0213
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
 38-470 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: 520.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrqqL----V 113
Cdd:COG0213   3 DIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSD-----IpgpkV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  114 DKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVP 193
Cdd:COG0213  78 DKHSTGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAP 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  194 ADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAM 273
Cdd:COG0213 158 ADKKLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDM 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  274 DKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVD 353
Cdd:COG0213 238 NQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGD 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445  354 PGLaralcsgspAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRR 433
Cdd:COG0213 318 PDV---------VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEK 388

                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503445  434 GTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAP 470
Cdd:COG0213 389 GEPLATIHANDEADAEEAAERLRAAYTIGDEPPEPPP 425
Y_phosphoryl TIGR02644
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated ...
 37-446 5.78e-159

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: 456.31  E-value: 5.78e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445     37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQqLVDKH 116
Cdd:TIGR02644   2 VDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGP-KVDKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    117 STGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADG 196
Cdd:TIGR02644  81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    197 ILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKP 276
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    277 LGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGL 356
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALAEDVLESGKALEKFRRFVEAQGGDPDV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    357 ARALcsgspaerrQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTP 436
Cdd:TIGR02644 321 IKNL---------DKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDP 391

                         410
                  ....*....|
gi 4503445    437 WLRVHRDGPA 446
Cdd:TIGR02644 392 LATLYSSDPI 401
deoA PRK05820
thymidine phosphorylase; Reviewed
 37-470 7.69e-159

thymidine phosphorylase; Reviewed


Pssm-ID: 180276 [Multi-domain]  Cd Length: 440  Bit Score: 457.37  E-value: 7.69e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQ-LVDK 115
Cdd:PRK05820   5 QEIIRKKRDGGALSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRDSGEVLDWSSLNLNGpIVDK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   116 HSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPAD 195
Cdd:PRK05820  85 HSTGGVGDKISLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYRAFPSNDRFREILKDVGVAIIGQTSDLAPAD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   196 GILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDK 275
Cdd:PRK05820 165 KRLYALRDVTATVESIPLITASILSKKLAEGLDALVLDVKVGSGAFMKTYEEARELARSMVEVANGAGVRTTALLTDMNQ 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   276 PLGRCVGHALEVEEALLCMDGA-GPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDP 354
Cdd:PRK05820 245 PLASSAGNALEVREAVEFLTGGyRPPRLVEVTMALAAEMLVLAGLAKDEAEARADLAAVLDSGKAAERFGRMVAAQGGPP 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   355 GLARALCSGspaerrqlLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRG 434
Cdd:PRK05820 325 DFVENYDKY--------LPTAPHTKPVYADRSGVLSAMDTRALGMAVVRLGGGRRRKGDPIDYSVGLTLHARLGDRVDAG 396

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 4503445   435 TPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAP 470
Cdd:PRK05820 397 EPLATLHADDEERFQEAAAALKAAIRIGDEAPEATP 432
T_phosphoryl TIGR02643
thymidine phosphorylase; Thymidine phosphorylase (alternate name: pyrimidine phosphorylase), ...
 38-471 5.19e-118

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: 353.28  E-value: 5.19e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445     38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEA-WRQQLVDKH 116
Cdd:TIGR02643   5 EIIRKKRDGHSLSDAEIAQFINGITDGSVSEGQIAAFAMAVFFNGMNRDERVALTLAMRDSGDVLDWRSLdLNGPVVDKH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    117 STGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADG 196
Cdd:TIGR02643  85 STGGVGDVVSLMLGPIVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYDIFPDPALFRRVVKDVGVAIIGQTADLAPADK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    197 ILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKP 276
Cdd:TIGR02643 165 RFYATRDVTATVESIPLITASILSKKLAAGLDALVMDVKVGNGAFMPTYEESEELARSLVDVANGAGVRTTALITDMNQP 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    277 LGRCVGHALEVEEALLCMDGA-GPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQgvdpg 355
Cdd:TIGR02643 245 LASAAGNAVEVRNAVDFLTGEkRNPRLEDVTMALAAEMLVSGGLAADEAEARAKLQAVLDSGRAAERFARMVAAL----- 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    356 laralcsGSPA---ER-RQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRL 431
Cdd:TIGR02643 320 -------GGPAdfvENpERYLATAPLIKPVYADREGYVSEMDTRALGMAVVALGGGRRKADDTIDYSVGLTDLLPLGDRV 392

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 4503445    432 RRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPS 471
Cdd:TIGR02643 393 EKGEPLAVVHAADESDAEEAAKRVKAAYRIADEAPESTPV 432
PRK06078 PRK06078
pyrimidine-nucleoside phosphorylase; Reviewed
 38-441 4.34e-116

pyrimidine-nucleoside phosphorylase; Reviewed


Pssm-ID: 180387 [Multi-domain]  Cd Length: 434  Bit Score: 348.23  E-value: 4.34e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWpEAWRQQLVDKHS 117
Cdd:PRK06078   5 DLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTIDL-SAIEGIKVDKHS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   118 TGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADGI 197
Cdd:PRK06078  84 TGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFIKLVNENKVAVIGQSGNLTPADKK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   198 LYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPL 277
Cdd:PRK06078 164 LYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTVEDAEELAHAMVRIGNNVGRNTMAVISDMSQPL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   278 GRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPgla 357
Cdd:PRK06078 244 GRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMVVLAGKAKTLEEAREHLIEVMNNGKALEKFKEFLSAQGGDA--- 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   358 ralcsgSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPW 437
Cdd:PRK06078 321 ------SVVDDPEKLPQAKYQIEVPAKESGYISELVADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESL 394


                 ....
gi 4503445   438 LRVH 441
Cdd:PRK06078 395 ATIY 398
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
 109-340 3.86e-65

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: 210.61  E-value: 3.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    109 RQQLVDKHSTGGVGDK---VSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCCIV 185
Cdd:pfam00591   1 LGDLVDIVGTGGDGDNtfnISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    186 GQSEQLVPADGILYAARDVTA-TVDSL--PLITA--------SILSKKLVEGLSALVVDVKFGGAAVFPN--QEQARELA 252
Cdd:pfam00591  80 FAPNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGdgLDEASLLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    253 KTLVGVGAsLGLRVAAALTAMDKPLGRCVGHALEV---EEALLCMDGA--GPPDL--RDLVTTLGGALLWLSGHAGTQAQ 325
Cdd:pfam00591 160 KTTVAELK-DGEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAahRDLVALNAGAALYLAGKADSLKE 238

                         250
                  ....*....|....*
gi 4503445    326 GAARVAAALDDGSAL 340
Cdd:pfam00591 239 GVAKALEVIDSGKAL 253
PRK04350 PRK04350
thymidine phosphorylase; Provisional
 29-466 7.35e-62

thymidine phosphorylase; Provisional


Pssm-ID: 235289 [Multi-domain]  Cd Length: 490  Bit Score: 209.28  E-value: 7.35e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    29 PSPEPKQLpELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPeaw 108
Cdd:PRK04350  75 HAPPPESL-SAIRKKIDGEKLDKEEIEAIIRDIVAGRYSDIELSAFLTASAINGLDMDEIEALTRAMVETGERLDWD--- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   109 RQQLVDKHSTGGV-GDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPgfNVIQSPEQMQVLLDQAGCCIV-G 186
Cdd:PRK04350 151 RPPVVDKHSIGGVpGNRTTLIVVPIVAAAGLTIPKTSSRAITSPAGTADTMEVLA--PVDLSVEEIKRVVEKVGGCLVwG 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   187 QSEQLVPADGIL----YAARdvtatVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASL 262
Cdd:PRK04350 229 GAVNLSPADDILirveRPLS-----IDPRGQLVASILSKKIAAGSTHVVIDIPVGPTAKVRSVEEARRLARLFEEVGDRL 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   263 GLRVAAALTAMDKPLGRCVGHALEVEEALLCM--DGAGPPDLRDLVTTLGGALLWLSGHAGTqAQGAARVAAALDDGSAL 340
Cdd:PRK04350 304 GLRVECAITDGSQPIGRGIGPALEARDVLAVLenDPDAPNDLREKSLRLAGILLEMGGVAPG-GEGYALAREILESGKAL 382

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   341 GRFERMLAAQGvdpglaralcsGSPAErrqlLPRAREQEELLAPADGTVELVRALPLAlvlhelGAGRsRAGEPLRLGVG 420
Cdd:PRK04350 383 EKFQEIIEAQG-----------GDSED----IPLGDHTHDVTAPRDGYVTAIDNRRLA------RIAR-LAGAPKDKGAG 440

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 4503445   421 AELLVDVGQRLRRGTPWLRVHRDGPAlsgpqsrALQEALVLSDRAP 466
Cdd:PRK04350 441 IDLHVKVGDKVKKGDPLYTIHAESEG-------ELDYAIELARRHP 479
Glycos_trans_3N pfam02885
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ...
 37-99 9.63e-17

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: 74.34  E-value: 9.63e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503445     37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSG 99
Cdd:pfam02885   1 KELIKKLRDGEDLTREEARAAMDGIMSGEATDAQIAAFLMALRMKGETAEEIAGLARAMRESG 63
PYNP_C smart00941
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
 389-462 1.16e-13

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: 66.02  E-value: 1.16e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503445     389 VELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLS 462
Cdd:smart00941   2 VTAIDARALGLAAVLLGAGRARKEDPIDYGVGIVLHKKLGDRVKKGEPLATIHANDEAELEEAAEALRAAITIS 75
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
46-350 3.60e-09

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 58.96  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    46 GGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPeawRQQLVDKHSTGGVGDK- 124
Cdd:PRK14607 205 GEDLSFEEAEDVMEDITDGNATDAQIAGFLTALRMKGETADELAGFASVMREKSRHIPAP---SPRTVDTCGTGGDGFGt 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   125 --VSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCCIVgQSEQLVPADGILYAAR 202
Cdd:PRK14607 282 fnISTTSAFVVAAAGVPVAKHGNRAVSSKSGSADVLEAL-GVKLEMTPEEAASVLRETGFSFL-FAPLFHPAMKHAAPAR 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   203 DV--TATVDSL--PLITASILSKKLVEglsalVVDVKFggaavfpnqeqARELAKTLVGVGASLGLrVAAALTAMDKpLG 278
Cdd:PRK14607 360 RElgIRTAFNLlgPLTNPARVKYQIVG-----VFDPSY-----------AEPLAQALQRLGTERAM-VVSGIDGYDE-IS 421

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   279 RCV-GHALEVEE----------------------------------ALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQ 323
Cdd:PRK14607 422 TCGpTQILELEDgeivtytfdpeelglkrvdpeelkggdpqenyrlAEDVLKGEPRRPQRDAVALNAGAALYLVGEADSI 501

                        330       340
                 ....*....|....*....|....*..
gi 4503445   324 AQGAARVAAALDDGSALGRFERMLAAQ 350
Cdd:PRK14607 502 KEGVGKALDLIDDGRAYKKLEEVMDLS 528
TrpD COG0547
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ...
 45-183 5.98e-09

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: 57.40  E-value: 5.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   45 DGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLewpEAWRQQLVDKHSTGGVGDK 124
Cdd:COG0547  11 EGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPV---PLPDGDVVDIVGTGGDGAN 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503445  125 ---VSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCC 183
Cdd:COG0547  88 tfnISTAAAFVAAAAGVPVAKHGNRSVSSKSGSADVLEAL-GVNLDLSPEQVARCLEEAGIG 148
PYNP_C pfam07831
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
 389-446 6.69e-06

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: 43.72  E-value: 6.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4503445    389 VELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLRVHRDGPA 446
Cdd:pfam07831   2 VSSIDAREIGMAAMELGAGRATKTDPIDYGVGIYLHKKLGDKVKKGEPLATIYANDEI 59
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 49-185 3.42e-05

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 46.17  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    49 LSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrQQLVDKHSTGGVGDK---V 125
Cdd:PRK09522 213 LSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPD---YLFADIVGTGGDGSNsinI 289

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445   126 SLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCCIV 185
Cdd:PRK09522 290 STASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAF-GINLDMNADKSRQALDELGVCFL 348
PLN02641 PLN02641
anthranilate phosphoribosyltransferase
 33-181 3.63e-05

anthranilate phosphoribosyltransferase


Pssm-ID: 215345 [Multi-domain]  Cd Length: 343  Bit Score: 45.88  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    33 PKQLPELIRMKRDGGRLSEADIRGFVAAVVNGsAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWpeawRQQL 112
Cdd:PLN02641   1 IASFRQLIESLIQGTDLTEEEAEAALDFLLDD-ADEAQISAFLVLLRAKGETFEEIAGLARAMIKRARKVDG----LVDA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503445   113 VDKHSTGGVG-DKV-----SLVLApalAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAG 181
Cdd:PLN02641  76 VDIVGTGGDGaNTVnistgSSILA---AACGAKVAKQGNRSSSSACGSADVLEAL-GVAIDLGPEGVKRCVEEVG 146
trpD PRK00188
anthranilate phosphoribosyltransferase; Provisional
 45-183 3.06e-04

anthranilate phosphoribosyltransferase; Provisional


Pssm-ID: 234682 [Multi-domain]  Cd Length: 339  Bit Score: 42.76  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503445    45 DGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAwrqqLVDKHSTGGVGDK 124
Cdd:PRK00188  12 EGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHAVPVPDPDD----AVDIVGTGGDGAN 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503445   125 -------VSLVlapaLAACGCKVPMISGRGL-GHTGGTlDKLESIpGFNVIQSPEQMQVLLDQAGCC 183
Cdd:PRK00188  88 tfnistaAAFV----AAAAGVKVAKHGNRSVsSKSGSA-DVLEAL-GVNLDLSPEQVARCLEEVGIG 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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