NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|500941435|ref|WP_012027066|]
View 

MULTISPECIES: pyrimidine-nucleoside phosphorylase [Streptococcus]

Protein Classification

pyrimidine-nucleoside phosphorylase( domain architecture ID 11482043)

pyrimidine-nucleoside phosphorylase catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK06078 PRK06078
pyrimidine-nucleoside phosphorylase; Reviewed
1-425 0e+00

pyrimidine-nucleoside phosphorylase; Reviewed


:

Pssm-ID: 180387 [Multi-domain]  Cd Length: 434  Bit Score: 788.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   1 MRAVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAIPGIKVD 80
Cdd:PRK06078   1 MRMVDLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTIDLSAIEGIKVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  81 KHSTGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLVKA 160
Cdd:PRK06078  81 KHSTGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFIKLVNENKVAVIGQSGNLTPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 161 DKLLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTDMS 240
Cdd:PRK06078 161 DKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTVEDAEELAHAMVRIGNNVGRNTMAVISDMS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 241 QPVGTSIGNRLEILEAIEILQGKGREDVTEFICELAQIMLGLANVEKSIEEVRQH----IDNGAALKKFEEMVRAQGGD- 315
Cdd:PRK06078 241 QPLGRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMVVLAGKAKTLEEAREHlievMNNGKALEKFKEFLSAQGGDa 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 316 --LEDLYRPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYAN 393
Cdd:PRK06078 321 svVDDPEKLPQAKYQIEVPAKESGYISELVADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESLATIYAN 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 500941435 394 ENISENMLTNFQKNVKIDKESVKTKEIIEIIS 425
Cdd:PRK06078 401 RENVEDVKAKFYKNIKISKEHVVAPELIHIII 432
 
Name Accession Description Interval E-value
PRK06078 PRK06078
pyrimidine-nucleoside phosphorylase; Reviewed
1-425 0e+00

pyrimidine-nucleoside phosphorylase; Reviewed


Pssm-ID: 180387 [Multi-domain]  Cd Length: 434  Bit Score: 788.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   1 MRAVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAIPGIKVD 80
Cdd:PRK06078   1 MRMVDLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTIDLSAIEGIKVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  81 KHSTGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLVKA 160
Cdd:PRK06078  81 KHSTGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFIKLVNENKVAVIGQSGNLTPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 161 DKLLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTDMS 240
Cdd:PRK06078 161 DKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTVEDAEELAHAMVRIGNNVGRNTMAVISDMS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 241 QPVGTSIGNRLEILEAIEILQGKGREDVTEFICELAQIMLGLANVEKSIEEVRQH----IDNGAALKKFEEMVRAQGGD- 315
Cdd:PRK06078 241 QPLGRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMVVLAGKAKTLEEAREHlievMNNGKALEKFKEFLSAQGGDa 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 316 --LEDLYRPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYAN 393
Cdd:PRK06078 321 svVDDPEKLPQAKYQIEVPAKESGYISELVADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESLATIYAN 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 500941435 394 ENISENMLTNFQKNVKIDKESVKTKEIIEIIS 425
Cdd:PRK06078 401 RENVEDVKAKFYKNIKISKEHVVAPELIHIII 432
DeoA COG0213
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
3-424 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: 652.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   3 AVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAIPGIKVDKH 82
Cdd:COG0213    1 AVDIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSDIPGPKVDKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  83 STGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLVKADK 162
Cdd:COG0213   81 STGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAPADK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 163 LLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTDMSQP 242
Cdd:COG0213  161 KLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDMNQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 243 VGTSIGNRLEILEAIEILQGKGREDVTEFICELAQIMLGLANVEKSIEE----VRQHIDNGAALKKFEEMVRAQGGD--- 315
Cdd:COG0213  241 LGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEarakLEEALASGKALEKFKEMVAAQGGDpdv 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 316 LEDLYRPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYANEN 395
Cdd:COG0213  321 VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEKGEPLATIHANDE 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 500941435 396 IS-ENMLTNFQKNVKIDKESVKTKEII-EII 424
Cdd:COG0213  401 ADaEEAAERLRAAYTIGDEPPEPPPLIyERI 431
Y_phosphoryl TIGR02644
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated ...
3-397 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: 586.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435    3 AVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAIPGIKVDKH 82
Cdd:TIGR02644   1 AVDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGPKVDKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   83 STGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLVKADK 162
Cdd:TIGR02644  81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  163 LLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTDMSQP 242
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  243 VGTSIGNRLEILEAIEILQGKGREDVTEFICELAQIMLGLANVEKSIEEVRQH----IDNGAALKKFEEMVRAQGGD--- 315
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALaedvLESGKALEKFRRFVEAQGGDpdv 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  316 LEDLYRPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYANEN 395
Cdd:TIGR02644 321 IKNLDKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDPLATLYSSDP 400

                  ..
gi 500941435  396 IS 397
Cdd:TIGR02644 401 IS 402
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
76-302 1.21e-43

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: 153.21  E-value: 1.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   76 GIKVDKHSTGGVGDK---VTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIkGYQIEVSQADFIKQVQDTGVAVIG 152
Cdd:pfam00591   2 GDLVDIVGTGGDGDNtfnISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  153 QSDNLVKADKLLYALRDVTA-TVDII--PLIAS--------SVMSKKIAAGADAILLDVTVGEGAFMKTV--EEARVLAQ 219
Cdd:pfam00591  81 APNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGDglDEASLLGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  220 TMVDLGKAvGRKTVAVLTDMSQPVGTSIGNRLEILEAIE-------ILQGKGREDVTEFICELAQIMLGLANVEKSIEE- 291
Cdd:pfam00591 161 TTVAELKD-GEITEYTLTPEDFGLGRATLEALEGGSPKEnadilkgVLGGKGSAAHRDLVALNAGAALYLAGKADSLKEg 239
                         250
                  ....*....|....
gi 500941435  292 ---VRQHIDNGAAL 302
Cdd:pfam00591 240 vakALEVIDSGKAL 253
PYNP_C smart00941
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
338-411 4.49e-20

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: 83.74  E-value: 4.49e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500941435   338 YIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYANENISENMLTNF-QKNVKID 411
Cdd:smart00941   1 YVTAIDARALGLAAVLLGAGRARKEDPIDYGVGIVLHKKLGDRVKKGEPLATIHANDEAELEEAAEAlRAAITIS 75
 
Name Accession Description Interval E-value
PRK06078 PRK06078
pyrimidine-nucleoside phosphorylase; Reviewed
1-425 0e+00

pyrimidine-nucleoside phosphorylase; Reviewed


Pssm-ID: 180387 [Multi-domain]  Cd Length: 434  Bit Score: 788.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   1 MRAVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAIPGIKVD 80
Cdd:PRK06078   1 MRMVDLIQKKRDGKELTTEEINFFIEGYTNGTIPDYQMSALAMAIYFKDMTDRERADLTMAMVNSGDTIDLSAIEGIKVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  81 KHSTGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLVKA 160
Cdd:PRK06078  81 KHSTGGVGDTTTLVLAPLVAAFGVPVAKMSGRGLGHTGGTIDKLESIKGFHVEISQEDFIKLVNENKVAVIGQSGNLTPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 161 DKLLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTDMS 240
Cdd:PRK06078 161 DKKLYALRDVTATVNSIPLIASSIMSKKIAAGADAIVLDVKTGAGAFMKTVEDAEELAHAMVRIGNNVGRNTMAVISDMS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 241 QPVGTSIGNRLEILEAIEILQGKGREDVTEFICELAQIMLGLANVEKSIEEVRQH----IDNGAALKKFEEMVRAQGGD- 315
Cdd:PRK06078 241 QPLGRAIGNALEVLEAIDTLQGKGPKDLTELVLTLGSQMVVLAGKAKTLEEAREHlievMNNGKALEKFKEFLSAQGGDa 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 316 --LEDLYRPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYAN 393
Cdd:PRK06078 321 svVDDPEKLPQAKYQIEVPAKESGYISELVADEIGLAAMLLGAGRATKEDEIDLAVGIVLRKKVGDSVKKGESLATIYAN 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 500941435 394 ENISENMLTNFQKNVKIDKESVKTKEIIEIIS 425
Cdd:PRK06078 401 RENVEDVKAKFYKNIKISKEHVVAPELIHIII 432
DeoA COG0213
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
3-424 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: 652.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   3 AVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAIPGIKVDKH 82
Cdd:COG0213    1 AVDIIRKKRDGGELTAEEIRFFIDGYTDGSIPDYQMAAFLMAVYFRGMTDEETAALTLAMRDSGDVLDLSDIPGPKVDKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  83 STGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLVKADK 162
Cdd:COG0213   81 STGGVGDKTSLVLAPLVAACGVPVPKMSGRGLGHTGGTLDKLESIPGFRTELSEEEFRRQVNEIGCAIIGQTGDLAPADK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 163 LLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTDMSQP 242
Cdd:COG0213  161 KLYALRDVTATVESIPLIASSIMSKKLAAGADALVLDVKVGSGAFMKTLEDARELAESMVDIGNGAGRKTVALITDMNQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 243 VGTSIGNRLEILEAIEILQGKGREDVTEFICELAQIMLGLANVEKSIEE----VRQHIDNGAALKKFEEMVRAQGGD--- 315
Cdd:COG0213  241 LGRAVGNALEVKEAIETLKGEGPEDLTELTLALGAEMLVLAGLAKDLEEarakLEEALASGKALEKFKEMVAAQGGDpdv 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 316 LEDLYRPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYANEN 395
Cdd:COG0213  321 VDDPELLPQAPVVREVKAPRSGYVSAIDARAIGLAAVLLGAGRATKEDPIDPAVGIVLLKKVGDKVEKGEPLATIHANDE 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 500941435 396 IS-ENMLTNFQKNVKIDKESVKTKEII-EII 424
Cdd:COG0213  401 ADaEEAAERLRAAYTIGDEPPEPPPLIyERI 431
Y_phosphoryl TIGR02644
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated ...
3-397 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: 586.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435    3 AVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAIPGIKVDKH 82
Cdd:TIGR02644   1 AVDIIRKKRDGKKLSDEEINFFINGYTNGEIPDYQMSALLMAIYFNGMTDEETAYLTKAMIDSGEVLDLSSLPGPKVDKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   83 STGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLVKADK 162
Cdd:TIGR02644  81 STGGVGDKVSLVLGPIVAACGVKVAKMSGRGLGHTGGTIDKLESIPGFRTELSEAEFIEIVNKVGLAIIGQTKDLAPADK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  163 LLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTDMSQP 242
Cdd:TIGR02644 161 KLYALRDVTGTVDSIPLIASSIMSKKLAAGADAIVLDVKVGSGAFMKTLEDAKELAKLMVEIGKGAGRKTSALLTDMNQP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  243 VGTSIGNRLEILEAIEILQGKGREDVTEFICELAQIMLGLANVEKSIEEVRQH----IDNGAALKKFEEMVRAQGGD--- 315
Cdd:TIGR02644 241 LGRAIGNALEVKEAVEFLKGEGPADLKELTLALAAEMLLLAGIAKTEKEARALaedvLESGKALEKFRRFVEAQGGDpdv 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  316 LEDLYRPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYANEN 395
Cdd:TIGR02644 321 IKNLDKLPKAKYKEEVKAEKSGYISEIDAEELGLAAVDLGAGRARKEDKIDHEAGIYLHKKTGDRVKKGDPLATLYSSDP 400

                  ..
gi 500941435  396 IS 397
Cdd:TIGR02644 401 IS 402
deoA PRK05820
thymidine phosphorylase; Reviewed
1-425 0e+00

thymidine phosphorylase; Reviewed


Pssm-ID: 180276 [Multi-domain]  Cd Length: 440  Bit Score: 513.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   1 MRAVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAI--PGIK 78
Cdd:PRK05820   2 FLAQEIIRKKRDGGALSDEEIDWFIDGYTDGTVSDGQIAALAMAIFFNGMTRPERVALTLAMRDSGEVLDWSSLnlNGPI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  79 VDKHSTGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLV 158
Cdd:PRK05820  82 VDKHSTGGVGDKISLMLAPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYRAFPSNDRFREILKDVGVAIIGQTSDLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 159 KADKLLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTD 238
Cdd:PRK05820 162 PADKRLYALRDVTATVESIPLITASILSKKLAEGLDALVLDVKVGSGAFMKTYEEARELARSMVEVANGAGVRTTALLTD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 239 MSQPVGTSIGNRLEILEAIEILQGKGR-EDVTEFICELAQIMLGLANVEKSIEE----VRQHIDNGAALKKFEEMVRAQG 313
Cdd:PRK05820 242 MNQPLASSAGNALEVREAVEFLTGGYRpPRLVEVTMALAAEMLVLAGLAKDEAEaradLAAVLDSGKAAERFGRMVAAQG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 314 GDLEDLYRPV----QVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIAT 389
Cdd:PRK05820 322 GPPDFVENYDkylpTAPHTKPVYADRSGVLSAMDTRALGMAVVRLGGGRRRKGDPIDYSVGLTLHARLGDRVDAGEPLAT 401
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 500941435 390 IYANENIS-ENMLTNFQKNVKI-DKESVKTKEIIEIIS 425
Cdd:PRK05820 402 LHADDEERfQEAAAALKAAIRIgDEAPEATPLIYRRIT 439
T_phosphoryl TIGR02643
thymidine phosphorylase; Thymidine phosphorylase (alternate name: pyrimidine phosphorylase), ...
1-424 1.49e-119

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: 355.21  E-value: 1.49e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435    1 MRAVDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSA--IPGIK 78
Cdd:TIGR02643   1 FLPQEIIRKKRDGHSLSDAEIAQFINGITDGSVSEGQIAAFAMAVFFNGMNRDERVALTLAMRDSGDVLDWRSldLNGPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   79 VDKHSTGGVGDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKGYQIEVSQADFIKQVQDTGVAVIGQSDNLV 158
Cdd:TIGR02643  81 VDKHSTGGVGDVVSLMLGPIVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYDIFPDPALFRRVVKDVGVAIIGQTADLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  159 KADKLLYALRDVTATVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVLTD 238
Cdd:TIGR02643 161 PADKRFYATRDVTATVESIPLITASILSKKLAAGLDALVMDVKVGNGAFMPTYEESEELARSLVDVANGAGVRTTALITD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  239 MSQPVGTSIGNRLEILEAIEILQGKGR----EDVTEFICELAQIMLGLANVEKSIE-EVRQHIDNGAALKKFEEMVRAQG 313
Cdd:TIGR02643 241 MNQPLASAAGNAVEVRNAVDFLTGEKRnprlEDVTMALAAEMLVSGGLAADEAEARaKLQAVLDSGRAAERFARMVAALG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  314 GDLEDLYRPVQVTQQV----PVLAEEDGYIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIAT 389
Cdd:TIGR02643 321 GPADFVENPERYLATAplikPVYADREGYVSEMDTRALGMAVVALGGGRRKADDTIDYSVGLTDLLPLGDRVEKGEPLAV 400
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 500941435  390 IYA-NENISENMLTNFQKNVKI-DKESVKTKEIIEII 424
Cdd:TIGR02643 401 VHAaDESDAEEAAKRVKAAYRIaDEAPESTPVVYRRI 437
PRK04350 PRK04350
thymidine phosphorylase; Provisional
4-392 3.72e-65

thymidine phosphorylase; Provisional


Pssm-ID: 235289 [Multi-domain]  Cd Length: 490  Bit Score: 216.21  E-value: 3.72e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   4 VDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDLSAipGIKVDKHS 83
Cdd:PRK04350  82 LSAIRKKIDGEKLDKEEIEAIIRDIVAGRYSDIELSAFLTASAINGLDMDEIEALTRAMVETGERLDWDR--PPVVDKHS 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  84 TGGV-GDKVTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIKgyQIEVSqADFIKQVQDT--GVAVIGQSDNLVKA 160
Cdd:PRK04350 160 IGGVpGNRTTLIVVPIVAAAGLTIPKTSSRAITSPAGTADTMEVLA--PVDLS-VEEIKRVVEKvgGCLVWGGAVNLSPA 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 161 DKLL----YALRdvtatVDIIPLIASSVMSKKIAAGADAILLDVTVGEGAFMKTVEEARVLAQTMVDLGKAVGRKTVAVL 236
Cdd:PRK04350 237 DDILirveRPLS-----IDPRGQLVASILSKKIAAGSTHVVIDIPVGPTAKVRSVEEARRLARLFEEVGDRLGLRVECAI 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 237 TDMSQPVGTSIGNRLEILEAIEILQGKGR--EDVTEFICELAQIML---GLANVEKSIEEVRQHIDNGAALKKFEEMVRA 311
Cdd:PRK04350 312 TDGSQPIGRGIGPALEARDVLAVLENDPDapNDLREKSLRLAGILLemgGVAPGGEGYALAREILESGKALEKFQEIIEA 391
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 312 QGGDLEDlyrPVQVTQQVPVLAEEDGYIVGLPALEFGLFAMKLGAGRavktdnlDYETGIVFHKKVGEAVSKGEQIATIY 391
Cdd:PRK04350 392 QGGDSED---IPLGDHTHDVTAPRDGYVTAIDNRRLARIARLAGAPK-------DKGAGIDLHVKVGDKVKKGDPLYTIH 461

                 .
gi 500941435 392 A 392
Cdd:PRK04350 462 A 462
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
76-302 1.21e-43

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: 153.21  E-value: 1.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   76 GIKVDKHSTGGVGDK---VTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIkGYQIEVSQADFIKQVQDTGVAVIG 152
Cdd:pfam00591   2 GDLVDIVGTGGDGDNtfnISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEAL-GINLDLTPEQVRKLLDEVGVGFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  153 QSDNLVKADKLLYALRDVTA-TVDII--PLIAS--------SVMSKKIAAGADAILLDVTVGEGAFMKTV--EEARVLAQ 219
Cdd:pfam00591  81 APNYHPAMKHVAPVRRELGIrTVFNLlgPLINParvkrqvlGVYSKELAEGLAEVLKDLGRERAAVVHGDglDEASLLGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  220 TMVDLGKAvGRKTVAVLTDMSQPVGTSIGNRLEILEAIE-------ILQGKGREDVTEFICELAQIMLGLANVEKSIEE- 291
Cdd:pfam00591 161 TTVAELKD-GEITEYTLTPEDFGLGRATLEALEGGSPKEnadilkgVLGGKGSAAHRDLVALNAGAALYLAGKADSLKEg 239
                         250
                  ....*....|....
gi 500941435  292 ---VRQHIDNGAAL 302
Cdd:pfam00591 240 vakALEVIDSGKAL 253
Glycos_trans_3N pfam02885
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ...
4-66 1.50e-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: 87.43  E-value: 1.50e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500941435    4 VDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATG 66
Cdd:pfam02885   1 KELIKKLRDGEDLTREEARAAMDGIMSGEATDAQIAAFLMALRMKGETAEEIAGLARAMRESG 63
PYNP_C pfam07831
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
338-410 2.80e-20

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: 84.16  E-value: 2.80e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500941435  338 YIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYAN-ENISENMLTNFQKNVKI 410
Cdd:pfam07831   1 YVSSIDAREIGMAAMELGAGRATKTDPIDYGVGIYLHKKLGDKVKKGEPLATIYANdEIRLEEAVKKLKKAIEI 74
PYNP_C smart00941
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
338-411 4.49e-20

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: 83.74  E-value: 4.49e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500941435   338 YIVGLPALEFGLFAMKLGAGRAVKTDNLDYETGIVFHKKVGEAVSKGEQIATIYANENISENMLTNF-QKNVKID 411
Cdd:smart00941   1 YVTAIDARALGLAAVLLGAGRARKEDPIDYGVGIVLHKKLGDRVKKGEPLATIHANDEAELEEAAEAlRAAITIS 75
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
4-314 2.98e-08

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 55.49  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   4 VDLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISdlTMSMVATGEQIDLSAIPGIKVDKHS 83
Cdd:PRK14607 196 KSYLKKLVEGEDLSFEEAEDVMEDITDGNATDAQIAGFLTALRMKGETADELA--GFASVMREKSRHIPAPSPRTVDTCG 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  84 TGGVGDK---VTLILAPLVASFDIPVAKMSGRGLGHTGGTLDKLESIkGYQIEVSQADFIKQVQDTGVAvigqsdnLVKA 160
Cdd:PRK14607 274 TGGDGFGtfnISTTSAFVVAAAGVPVAKHGNRAVSSKSGSADVLEAL-GVKLEMTPEEAASVLRETGFS-------FLFA 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 161 DKLLYALRDVTA------TVDIIPLIASsvmskkIAAGADAILLDVTVGEGAFmktveeARVLAQTMVDLGkaVGRKTVA 234
Cdd:PRK14607 346 PLFHPAMKHAAParrelgIRTAFNLLGP------LTNPARVKYQIVGVFDPSY------AEPLAQALQRLG--TERAMVV 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 235 VLTDMSQPVGTSIGNRLEILE-----------------------------------AIEILQGKGREDVTEFICELAQIM 279
Cdd:PRK14607 412 SGIDGYDEISTCGPTQILELEdgeivtytfdpeelglkrvdpeelkggdpqenyrlAEDVLKGEPRRPQRDAVALNAGAA 491
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 500941435 280 LGLANVEKSIEE----VRQHIDNGAALKKFEEMVRAQGG 314
Cdd:PRK14607 492 LYLVGEADSIKEgvgkALDLIDDGRAYKKLEEVMDLSKT 530
trpD PRK00188
anthranilate phosphoribosyltransferase; Provisional
5-311 2.53e-07

anthranilate phosphoribosyltransferase; Provisional


Pssm-ID: 234682 [Multi-domain]  Cd Length: 339  Bit Score: 52.00  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435   5 DLIQKKRDGLELSSEEIKWLIDGYVAGTVPDYQMSALAMAIYFKGMSTREISDLTMSMVATGEQIDlsaIPGIKVDKHST 84
Cdd:PRK00188   5 ELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHAVPVP---DPDDAVDIVGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435  85 GGVGDK---VTLILAPLVASFDIPVAKMSGRGL-GHTGGTlDKLESIkGYQIEVSQADFIKQVQDTGVAvigqsdnlvka 160
Cdd:PRK00188  82 GGDGANtfnISTAAAFVAAAAGVKVAKHGNRSVsSKSGSA-DVLEAL-GVNLDLSPEQVARCLEEVGIG----------- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 161 dkLLYA------LRDV--------TATV-DII-PLIAssvmskkiAAGADAILLdvtvgeGAFMKtvEEARVLAQTMVDL 224
Cdd:PRK00188 149 --FLFAplyhpaMKHVapvrkelgIRTIfNLLgPLTN--------PARPKRQLI------GVYSP--DLLEPMAEVLKRL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500941435 225 G--KAV--------------GRKTVAVLTD-------------------MSQPVGtsiGNRLEILEAI-EILQGKGREDV 268
Cdd:PRK00188 211 GskRALvvhgsdgldeisltGPTTVAELKDgeireytltpedfglprapLEDLRG---GDPEENAAILrAVLQGKGPGAA 287
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 500941435 269 TEFICELAQIMLGLANVEKSIEE----VRQHIDNGAALKKFEEMVRA 311
Cdd:PRK00188 288 RDAVLLNAAAALYVAGKADDLKEgvelAREAIDSGAALAKLEELVAF 334
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH