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Conserved domains on  [gi|67477361|sp|P19971|]
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RecName: Full=Thymidine phosphorylase; Short=TP; AltName: Full=Gliostatin; AltName: Full=Platelet-derived endothelial cell growth factor; Short=PD-ECGF; AltName: Full=TdRPase; Flags: Precursor

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 67477361  38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrqqL----V 113
Cdd:COG0213   3 DIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSD-----IpgpkV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 114 DKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVP 193
Cdd:COG0213  78 DKHSTGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 194 ADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAM 273
Cdd:COG0213 158 ADKKLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDM 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 274 DKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVD 353
Cdd:COG0213 238 NQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGD 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 354 PGLaralcsgspAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRR 433
Cdd:COG0213 318 PDV---------VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEK 388
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 67477361 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 67477361  38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrqqL----V 113
Cdd:COG0213   3 DIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSD-----IpgpkV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 114 DKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVP 193
Cdd:COG0213  78 DKHSTGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 194 ADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAM 273
Cdd:COG0213 158 ADKKLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDM 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 274 DKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVD 353
Cdd:COG0213 238 NQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGD 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 354 PGLaralcsgspAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRR 433
Cdd:COG0213 318 PDV---------VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEK 388
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 67477361 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 67477361    37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQqLVDKH 116
Cdd:TIGR02644   2 VDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGP-KVDKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   117 STGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADG 196
Cdd:TIGR02644  81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   197 ILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKP 276
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   277 LGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGL 356
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALAEDVLESGKALEKFRRFVEAQGGDPDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   357 ARALcsgspaerrQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTP 436
Cdd:TIGR02644 321 IKNL---------DKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDP 391
                         410
                  ....*....|
gi 67477361   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 67477361   37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQ-LVDK 115
Cdd:PRK05820   5 QEIIRKKRDGGALSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRDSGEVLDWSSLNLNGpIVDK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  116 HSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPAD 195
Cdd:PRK05820  85 HSTGGVGDKISLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYRAFPSNDRFREILKDVGVAIIGQTSDLAPAD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  196 GILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDK 275
Cdd:PRK05820 165 KRLYALRDVTATVESIPLITASILSKKLAEGLDALVLDVKVGSGAFMKTYEEARELARSMVEVANGAGVRTTALLTDMNQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  276 PLGRCVGHALEVEEALLCMDGA-GPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDP 354
Cdd:PRK05820 245 PLASSAGNALEVREAVEFLTGGyRPPRLVEVTMALAAEMLVLAGLAKDEAEARADLAAVLDSGKAAERFGRMVAAQGGPP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  355 GLARALCSGspaerrqlLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRG 434
Cdd:PRK05820 325 DFVENYDKY--------LPTAPHTKPVYADRSGVLSAMDTRALGMAVVRLGGGRRRKGDPIDYSVGLTLHARLGDRVDAG 396
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 67477361  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 67477361   109 RQQLVDKHSTGGVGDK---VSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCCIV 185
Cdd:pfam00591   1 LGDLVDIVGTGGDGDNtfnISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   186 GQSEQLVPADGILYAARDVTA-TVDSL--PLITA--------SILSKKLVEGLSALVVDVKFGGAAVFPN--QEQARELA 252
Cdd:pfam00591  80 FAPNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGdgLDEASLLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   253 KTLVGVGAsLGLRVAAALTAMDKPLGRCVGHALEV---EEALLCMDGA--GPPDL--RDLVTTLGGALLWLSGHAGTQAQ 325
Cdd:pfam00591 160 KTTVAELK-DGEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAahRDLVALNAGAALYLAGKADSLKE 238
                         250
                  ....*....|....*
gi 67477361   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 67477361    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 67477361  38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrqqL----V 113
Cdd:COG0213   3 DIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSD-----IpgpkV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 114 DKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVP 193
Cdd:COG0213  78 DKHSTGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 194 ADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAM 273
Cdd:COG0213 158 ADKKLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDM 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 274 DKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVD 353
Cdd:COG0213 238 NQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEARAKLEEALASGKALEKFKEMVAAQGGD 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361 354 PGLaralcsgspAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRR 433
Cdd:COG0213 318 PDV---------VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEK 388
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 67477361 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 67477361    37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQqLVDKH 116
Cdd:TIGR02644   2 VDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGP-KVDKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   117 STGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADG 196
Cdd:TIGR02644  81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   197 ILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKP 276
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   277 LGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGL 356
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALAEDVLESGKALEKFRRFVEAQGGDPDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   357 ARALcsgspaerrQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTP 436
Cdd:TIGR02644 321 IKNL---------DKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDP 391
                         410
                  ....*....|
gi 67477361   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 67477361   37 PELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQ-LVDK 115
Cdd:PRK05820   5 QEIIRKKRDGGALSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRDSGEVLDWSSLNLNGpIVDK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  116 HSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPAD 195
Cdd:PRK05820  85 HSTGGVGDKISLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYRAFPSNDRFREILKDVGVAIIGQTSDLAPAD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  196 GILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDK 275
Cdd:PRK05820 165 KRLYALRDVTATVESIPLITASILSKKLAEGLDALVLDVKVGSGAFMKTYEEARELARSMVEVANGAGVRTTALLTDMNQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  276 PLGRCVGHALEVEEALLCMDGA-GPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDP 354
Cdd:PRK05820 245 PLASSAGNALEVREAVEFLTGGyRPPRLVEVTMALAAEMLVLAGLAKDEAEARADLAAVLDSGKAAERFGRMVAAQGGPP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  355 GLARALCSGspaerrqlLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRG 434
Cdd:PRK05820 325 DFVENYDKY--------LPTAPHTKPVYADRSGVLSAMDTRALGMAVVRLGGGRRRKGDPIDYSVGLTLHARLGDRVDAG 396
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 67477361  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 67477361    38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEA-WRQQLVDKH 116
Cdd:TIGR02643   5 EIIRKKRDGHSLSDAEIAQFINGITDGSVSEGQIAAFAMAVFFNGMNRDERVALTLAMRDSGDVLDWRSLdLNGPVVDKH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   117 STGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADG 196
Cdd:TIGR02643  85 STGGVGDVVSLMLGPIVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYDIFPDPALFRRVVKDVGVAIIGQTADLAPADK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   197 ILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKP 276
Cdd:TIGR02643 165 RFYATRDVTATVESIPLITASILSKKLAAGLDALVMDVKVGNGAFMPTYEESEELARSLVDVANGAGVRTTALITDMNQP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   277 LGRCVGHALEVEEALLCMDGA-GPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQgvdpg 355
Cdd:TIGR02643 245 LASAAGNAVEVRNAVDFLTGEkRNPRLEDVTMALAAEMLVSGGLAADEAEARAKLQAVLDSGRAAERFARMVAAL----- 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   356 laralcsGSPA---ER-RQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRL 431
Cdd:TIGR02643 320 -------GGPAdfvENpERYLATAPLIKPVYADREGYVSEMDTRALGMAVVALGGGRRKADDTIDYSVGLTDLLPLGDRV 392
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 67477361   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 67477361   38 ELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWpEAWRQQLVDKHS 117
Cdd:PRK06078   5 DLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTIDL-SAIEGIKVDKHS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  118 TGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADGI 197
Cdd:PRK06078  84 TGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFIKLVNENKVAVIGQSGNLTPADKK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  198 LYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPL 277
Cdd:PRK06078 164 LYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTVEDAEELAHAMVRIGNNVGRNTMAVISDMSQPL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  278 GRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPgla 357
Cdd:PRK06078 244 GRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMVVLAGKAKTLEEAREHLIEVMNNGKALEKFKEFLSAQGGDA--- 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  358 ralcsgSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPW 437
Cdd:PRK06078 321 ------SVVDDPEKLPQAKYQIEVPAKESGYISELVADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESL 394

                 ....
gi 67477361  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 67477361   109 RQQLVDKHSTGGVGDK---VSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCCIV 185
Cdd:pfam00591   1 LGDLVDIVGTGGDGDNtfnISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   186 GQSEQLVPADGILYAARDVTA-TVDSL--PLITA--------SILSKKLVEGLSALVVDVKFGGAAVFPN--QEQARELA 252
Cdd:pfam00591  80 FAPNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGdgLDEASLLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361   253 KTLVGVGAsLGLRVAAALTAMDKPLGRCVGHALEV---EEALLCMDGA--GPPDL--RDLVTTLGGALLWLSGHAGTQAQ 325
Cdd:pfam00591 160 KTTVAELK-DGEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAahRDLVALNAGAALYLAGKADSLKE 238
                         250
                  ....*....|....*
gi 67477361   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 67477361   29 PSPEPKQLpELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPeaw 108
Cdd:PRK04350  75 HAPPPESL-SAIRKKIDGEKLDKEEIEAIIRDIVAGRYSDIELSAFLTASAINGLDMDEIEALTRAMVETGERLDWD--- 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  109 RQQLVDKHSTGGV-GDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPgfNVIQSPEQMQVLLDQAGCCIV-G 186
Cdd:PRK04350 151 RPPVVDKHSIGGVpGNRTTLIVVPIVAAAGLTIPKTSSRAITSPAGTADTMEVLA--PVDLSVEEIKRVVEKVGGCLVwG 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  187 QSEQLVPADGIL----YAARdvtatVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASL 262
Cdd:PRK04350 229 GAVNLSPADDILirveRPLS-----IDPRGQLVASILSKKIAAGSTHVVIDIPVGPTAKVRSVEEARRLARLFEEVGDRL 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  263 GLRVAAALTAMDKPLGRCVGHALEVEEALLCM--DGAGPPDLRDLVTTLGGALLWLSGHAGTqAQGAARVAAALDDGSAL 340
Cdd:PRK04350 304 GLRVECAITDGSQPIGRGIGPALEARDVLAVLenDPDAPNDLREKSLRLAGILLEMGGVAPG-GEGYALAREILESGKAL 382
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  341 GRFERMLAAQGvdpglaralcsGSPAErrqlLPRAREQEELLAPADGTVELVRALPLAlvlhelGAGRsRAGEPLRLGVG 420
Cdd:PRK04350 383 EKFQEIIEAQG-----------GDSED----IPLGDHTHDVTAPRDGYVTAIDNRRLA------RIAR-LAGAPKDKGAG 440
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 67477361  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 67477361    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 67477361    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 67477361   46 GGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPeawRQQLVDKHSTGGVGDK- 124
Cdd:PRK14607 205 GEDLSFEEAEDVMEDITDGNATDAQIAGFLTALRMKGETADELAGFASVMREKSRHIPAP---SPRTVDTCGTGGDGFGt 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  125 --VSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIpGFNVIQSPEQMQVLLDQAGCCIVgQSEQLVPADGILYAAR 202
Cdd:PRK14607 282 fnISTTSAFVVAAAGVPVAKHGNRAVSSKSGSADVLEAL-GVKLEMTPEEAASVLRETGFSFL-FAPLFHPAMKHAAPAR 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  203 DV--TATVDSL--PLITASILSKKLVEglsalVVDVKFggaavfpnqeqARELAKTLVGVGASLGLrVAAALTAMDKpLG 278
Cdd:PRK14607 360 RElgIRTAFNLlgPLTNPARVKYQIVG-----VFDPSY-----------AEPLAQALQRLGTERAM-VVSGIDGYDE-IS 421
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  279 RCV-GHALEVEE----------------------------------ALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQ 323
Cdd:PRK14607 422 TCGpTQILELEDgeivtytfdpeelglkrvdpeelkggdpqenyrlAEDVLKGEPRRPQRDAVALNAGAALYLVGEADSI 501
                        330       340
                 ....*....|....*....|....*..
gi 67477361  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 67477361  45 DGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLewpEAWRQQLVDKHSTGGVGDK 124
Cdd:COG0547  11 EGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPV---PLPDGDVVDIVGTGGDGAN 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67477361 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 67477361   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 67477361   49 LSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEawrQQLVDKHSTGGVGDK---V 125
Cdd:PRK09522 213 LSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPD---YLFADIVGTGGDGSNsinI 289
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67477361  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 67477361   33 PKQLPELIRMKRDGGRLSEADIRGFVAAVVNGsAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWpeawRQQL 112
Cdd:PLN02641   1 IASFRQLIESLIQGTDLTEEEAEAALDFLLDD-ADEAQISAFLVLLRAKGETFEEIAGLARAMIKRARKVDG----LVDA 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67477361  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 67477361   45 DGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAwrqqLVDKHSTGGVGDK 124
Cdd:PRK00188  12 EGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHAVPVPDPDD----AVDIVGTGGDGAN 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67477361  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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