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Conserved domains on  [gi|1091062888|gb|OHP97421|]
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ribose-phosphate pyrophosphokinase [Staphylococcus sp. HMSC063F03]

Protein Classification

ribose-phosphate pyrophosphokinase( domain architecture ID 11479511)

ribose-phosphate pyrophosphokinase catalyzes the transfer of the pyrophosphoryl group from ATP to the 1-hydroxyl of ribose-5-phosphate to form the the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP)

EC:  2.7.6.1
Gene Ontology:  GO:0000287|GO:0004749|GO:0005737|GO:0005524|GO:0009156|GO:0016301|GO:0016310|GO:0006015|GO:0009165
PubMed:  7593598

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
11-321 0e+00

ribose-phosphate diphosphokinase;


:

Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 547.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  11 MKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAA 90
Cdd:PRK01259    1 MKLFAGNANPELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPTNDNLMELLIMIDALKRASAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  91 NINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENDpdiNP 170
Cdd:PRK01259   81 RITAVIPYFGYARQDRKARSRVPITAKLVANLLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK---NL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 171 EECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDKGAK 250
Cdd:PRK01259  158 ENLVVVSPDVGGVVRARALAKRLDADLAIIDKRRPRANVSEVMNIIGDVEGRDCILVDDMIDTAGTLCKAAEALKERGAK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091062888 251 EVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQL-EENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PRK01259  238 SVYAYATHPVLSGGAIERIENSVIDELVVTDSIPLsEEAKKCDKIRVLSVAPLLAEAIRRISNEESVSSLFD 309
 
Name Accession Description Interval E-value
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
11-321 0e+00

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 547.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  11 MKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAA 90
Cdd:PRK01259    1 MKLFAGNANPELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPTNDNLMELLIMIDALKRASAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  91 NINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENDpdiNP 170
Cdd:PRK01259   81 RITAVIPYFGYARQDRKARSRVPITAKLVANLLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK---NL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 171 EECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDKGAK 250
Cdd:PRK01259  158 ENLVVVSPDVGGVVRARALAKRLDADLAIIDKRRPRANVSEVMNIIGDVEGRDCILVDDMIDTAGTLCKAAEALKERGAK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091062888 251 EVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQL-EENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PRK01259  238 SVYAYATHPVLSGGAIERIENSVIDELVVTDSIPLsEEAKKCDKIRVLSVAPLLAEAIRRISNEESVSSLFD 309
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 8-321 0e+00

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 528.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   8 NSSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRA 87
Cdd:COG0462     1 MKDLKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMELLIMIDALKRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  88 SAANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENdpd 167
Cdd:COG0462    81 SARRITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKS--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 168 INPEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDK 247
Cdd:COG0462   158 KDLEDLVVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091062888 248 GAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:COG0462   238 GAKSVYAAATHGVLSGPAVERLENSPIDELVVTDTIPLPEEKRCDKIKVLSVAPLLAEAIRRIHEGESVSSLFD 311
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 11-321 9.53e-149

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 420.15  E-value: 9.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  11 MKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIV-QPTSYPVNLHLMELLIMIDACKRASA 89
Cdd:TIGR01251   1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIqQSTSAPVNDNLMELLIMIDALKRASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  90 ANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFendPDIN 169
Cdd:TIGR01251  81 KSITAVIPYYGYARQDKKFKSREPISAKLVANLLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYL---KKKI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 170 PEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRP-KPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDKG 248
Cdd:TIGR01251 158 LDNPVVVSPDAGGVERAKKVADALGCPLAIIDKRRIsATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091062888 249 AKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEenRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:TIGR01251 238 AKRVIAAATHGVFSGPAIERIANAGVEEVIVTNTIPHE--KHKPKVSVISVAPLIAEAIRRIHNNESVSSLFD 308
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 11-127 4.52e-76

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 228.46  E-value: 4.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  11 MKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAA 90
Cdd:pfam13793   1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPVNDNLMELLIMIDALKRASAK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1091062888  91 NINIVVPYYGYARQDRKARSREPITAKLVANLIETAG 127
Cdd:pfam13793  81 RITAVIPYFGYARQDRKDKPREPITAKLVADLLEAAG 117
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 155-282 1.65e-15

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 72.04  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 155 VPILAQHFENDPDINPeecVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVM------NIVGDIEGRTAiiid 228
Cdd:cd06223     2 GRLLAEEIREDLLEPD---VVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEpyglelPLGGDVKGKRVllvd 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1091062888 229 diiDTAGTITLAAQALKDKGAKEVYACCTHPVLSGPAkeRIENSAIKQLIVTNS 282
Cdd:cd06223    79 dviATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA--RELASPGDPVYSLFT 130
 
Name Accession Description Interval E-value
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
11-321 0e+00

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 547.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  11 MKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAA 90
Cdd:PRK01259    1 MKLFAGNANPELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPTNDNLMELLIMIDALKRASAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  91 NINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENDpdiNP 170
Cdd:PRK01259   81 RITAVIPYFGYARQDRKARSRVPITAKLVANLLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK---NL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 171 EECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDKGAK 250
Cdd:PRK01259  158 ENLVVVSPDVGGVVRARALAKRLDADLAIIDKRRPRANVSEVMNIIGDVEGRDCILVDDMIDTAGTLCKAAEALKERGAK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091062888 251 EVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQL-EENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PRK01259  238 SVYAYATHPVLSGGAIERIENSVIDELVVTDSIPLsEEAKKCDKIRVLSVAPLLAEAIRRISNEESVSSLFD 309
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 8-321 0e+00

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 528.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   8 NSSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRA 87
Cdd:COG0462     1 MKDLKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMELLIMIDALKRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  88 SAANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENdpd 167
Cdd:COG0462    81 SARRITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKS--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 168 INPEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDK 247
Cdd:COG0462   158 KDLEDLVVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091062888 248 GAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:COG0462   238 GAKSVYAAATHGVLSGPAVERLENSPIDELVVTDTIPLPEEKRCDKIKVLSVAPLLAEAIRRIHEGESVSSLFD 311
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
9-321 2.00e-164

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 460.41  E-value: 2.00e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   9 SSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRAS 88
Cdd:PRK02269    4 SDLKLFALSSNKELAEKVAQEIGIELGKSSVRQFSDGEIQVNIEESIRGHHVFILQSTSSPVNDNLMEILIMVDALKRAS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  89 AANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFEnDPDI 168
Cdd:PRK02269   84 AESINVVMPYYGYARQDRKARSREPITSKLVANMLEVAGVDRLLTVDLHAAQIQGFFDIPVDHLMGAPLIADYFD-RRGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 169 NPEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRP--KPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKD 246
Cdd:PRK02269  163 VGDDVVVVSPDHGGVTRARKLAQFLKTPIAIIDKRRSvdKMNTSEVMNIIGNVKGKKCILIDDMIDTAGTICHAADALAE 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091062888 247 KGAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PRK02269  243 AGATEVYASCTHPVLSGPALDNIQKSAIEKLVVLDTIYLPEERLIDKIEQISIADLLGEAIIRIHEKRPLSPLFE 317
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 11-321 9.53e-149

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 420.15  E-value: 9.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  11 MKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIV-QPTSYPVNLHLMELLIMIDACKRASA 89
Cdd:TIGR01251   1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIqQSTSAPVNDNLMELLIMIDALKRASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  90 ANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFendPDIN 169
Cdd:TIGR01251  81 KSITAVIPYYGYARQDKKFKSREPISAKLVANLLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYL---KKKI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 170 PEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRP-KPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDKG 248
Cdd:TIGR01251 158 LDNPVVVSPDAGGVERAKKVADALGCPLAIIDKRRIsATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091062888 249 AKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEenRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:TIGR01251 238 AKRVIAAATHGVFSGPAIERIANAGVEEVIVTNTIPHE--KHKPKVSVISVAPLIAEAIRRIHNNESVSSLFD 308
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 20-321 2.14e-138

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 393.68  E-value: 2.14e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  20 EPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAANINIVVPYY 99
Cdd:PLN02369    1 PALSQEIACYLGLELGKITIKRFADGEIYVQLQESVRGCDVFLVQPTCPPANENLMELLIMIDACRRASAKRITAVIPYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 100 GYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENDpDINPEECVVVSPD 179
Cdd:PLN02369   81 GYARADRKTQGRESIAAKLVANLITEAGADRVLACDLHSGQSMGYFDIPVDHVYGQPVILDYLASK-TISSPDLVVVSPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 180 HGGVTRARKLADILK-TPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDKGAKEVYACCTH 258
Cdd:PLN02369  160 VGGVARARAFAKKLSdAPLAIVDKRRQGHNVAEVMNLIGDVKGKVAIMVDDMIDTAGTITKGAALLHQEGAREVYACATH 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091062888 259 PVLSGPAKERIENSAIKQLIVTNSIQLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PLN02369  240 AVFSPPAIERLSSGLFQEVIVTNTIPVSEKNYFPQLTVLSVANLLGETIWRVHDDCSVSSIFD 302
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 1-320 1.39e-137

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 392.95  E-value: 1.39e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   1 MLNNEYKNSSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIM 80
Cdd:PRK02812   12 QLPLLSDNNRLRLFSGSSNPALAQEVARYLGMDLGPMIRKRFADGELYVQIQESIRGCDVYLIQPTCAPVNDHLMELLIM 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  81 IDACKRASAANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQ 160
Cdd:PRK02812   92 VDACRRASARQITAVIPYYGYARADRKTAGRESITAKLVANLITKAGADRVLAMDLHSAQIQGYFDIPCDHVYGSPVLLD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 161 HFENDpdiNPEECVVVSPDHGGVTRARKLADILK-TPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITL 239
Cdd:PRK02812  172 YLASK---NLEDIVVVSPDVGGVARARAFAKKLNdAPLAIIDKRRQAHNVAEVLNVIGDVKGKTAILVDDMIDTGGTICE 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 240 AAQALKDKGAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVL 319
Cdd:PRK02812  249 GARLLRKEGAKQVYACATHAVFSPPAIERLSSGLFEEVIVTNTIPVPEERRFPQLKVLSVANMLGEAIWRIHEESSVSSM 328


                  .
gi 1091062888 320 F 320
Cdd:PRK02812  329 F 329
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 6-320 1.22e-126

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 364.83  E-value: 1.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   6 YKNSSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACK 85
Cdd:PRK02458    5 YADKQIKLFSLNSNLEIAEKIAQAAGVPLGKLSSRQFSDGEIMINIEESVRGDDIYIIQSTSFPVNDHLWELLIMIDACK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  86 RASAANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFeND 165
Cdd:PRK02458   85 RASANTVNVVLPYFGYARQDRIAKPREPITAKLVANMLVKAGVDRVLTLDLHAVQVQGFFDIPVDNLFTVPLFAKHY-CK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 166 PDINPEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMnIVGDIEGRTAIIIDDIIDTAGTITLAAQALK 245
Cdd:PRK02458  164 KGLSGSDVVVVSPKNSGIKRARSLAEYLDAPIAIIDYAQDDSEREEGY-IIGDVAGKKAILIDDILNTGKTFAEAAKIVE 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091062888 246 DKGAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIqLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLF 320
Cdd:PRK02458  243 REGATEIYAVASHGLFAGGAAEVLENAPIKEILVTDSV-ATKERVPKNVTYLSASELIADAIIRIHERKPLSPLF 316
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
22-321 1.77e-123

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 356.18  E-value: 1.77e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  22 LAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAANINIVVPYYGY 101
Cdd:PRK03092    1 LAEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQSHTAPINKWLMEQLIMIDALKRASAKRITVVLPFYPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 102 ARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENdpDINPEECVVVSPDHG 181
Cdd:PRK03092   81 ARQDKKHRGREPISARLVADLFKTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRD--KYDLDNVTVVSPDAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 182 GVTRARKLADIL-KTPIAIIDKRRP--KPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDKGAKEVYACCTH 258
Cdd:PRK03092  159 RVRVAEQWADRLgGAPLAFIHKTRDptVPNQVVANRVVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAATH 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091062888 259 PVLSGPAKERIENSAIKQLIVTNSIQLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PRK03092  239 GVLSGPAAERLKNCGAREVVVTDTLPIPEEKRFDKLTVLSIAPLLARAIREVFEDGSVTSLFD 301
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
9-320 2.58e-116

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 338.44  E-value: 2.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   9 SSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRAS 88
Cdd:PRK04923    5 RNLLVFSGNANKPLAQSICKELGVRMGKALVTRFSDGEVQVEIEESVRRQEVFVIQPTCAPSAENLMELLVLIDALKRAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  89 AANINIVVPYYGYARQDRKARS-REPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQhfendpD 167
Cdd:PRK04923   85 AASVTAVIPYFGYSRQDRRMRSsRVPITAKVAAKMISAMGADRVLTVDLHADQIQGFFDVPVDNVYASPLLLA------D 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 168 I----NPEECVVVSPDHGGVTRARKLADIL-KTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQ 242
Cdd:PRK04923  159 IwrayGTDNLIVVSPDVGGVVRARAVAKRLdDADLAIIDKRRPRANVATVMNIIGDVQGKTCVLVDDLVDTAGTLCAAAA 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091062888 243 ALKDKGAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEEN-RKPNNTKELSVAGLIAKAIIRVYERESVSVLF 320
Cdd:PRK04923  239 ALKQRGALKVVAYITHPVLSGPAVDNINNSQLDELVVTDTIPLSEAaRACAKIRQLSVAELLAETIRRIAFGESVSSLY 317
PTZ00145 PTZ00145
phosphoribosylpyrophosphate synthetase; Provisional
 13-321 1.13e-105

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 240290 [Multi-domain]  Cd Length: 439  Bit Score: 315.66  E-value: 1.13e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  13 IFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAANI 92
Cdd:PTZ00145  122 LFSGSSNPLLSKNIADHLGTILGRVHLKRFADGEVSMQFLESIRGKDVYIIQPTCPPVNENLIELLLMISTCRRASAKKI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  93 NIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFD--IPIDHLMGVPILAQHFENDPDINP 170
Cdd:PTZ00145  202 TAVIPYYGYARQDRKLSSRVPISAADVARMIEAMGVDRVVAIDLHSGQIQGFFGprVPVDNLEAQLIGLDYFTKKDLYKP 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 171 eecVVVSPDHGGVTRARKLAD------ILKTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQAL 244
Cdd:PTZ00145  282 ---VIVSPDAGGVYRARKFQDglnhrgISDCGIAMLIKQRTKPNEIEKMDLVGNVYDSDVIIVDDMIDTSGTLCEAAKQL 358

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091062888 245 KDKGAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEENRK--PNNTKeLSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PTZ00145  359 KKHGARRVFAFATHGLFSGPAIERIEASPLEEVVVTDTVKSNKNIDscKKITK-LSVSVLVADAIRRIHQKESLNDLFN 436
PRK00553 PRK00553
ribose-phosphate pyrophosphokinase; Provisional
 8-320 9.01e-87

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 179062 [Multi-domain]  Cd Length: 332  Bit Score: 263.70  E-value: 9.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   8 NSSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRA 87
Cdd:PRK00553    7 KSNHVIFSLSKAKKLVDSICRKLSMKPGEIVIQKFADGETYIRFDESVRNKDVVIFQSTCSPVNDSLMELLIAIDALKRG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  88 SAANINIVVPYYGYARQDRKARSREPITAKLVANLIETAGANRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENDPD 167
Cdd:PRK00553   87 SAKSITAILPYYGYARQDRKTAGREPITSKLVADLLTKAGVTRVTLTDIHSDQTQGFFDIPVDILRTYHVFLSRVLELLG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 168 InpEECVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVMNIVGDIEGRTAIIIDDIIDTAGTITLAAQALKDK 247
Cdd:PRK00553  167 K--KDLVVVSPDYGGVKRARLIAESLELPLAIIDKRRPKHNVAESINVLGEVKNKNCLIVDDMIDTGGTVIAAAKLLKKQ 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091062888 248 GAKEVYACCTHPVLSGPAKERIENSAIKQLI----VTNSIQLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLF 320
Cdd:PRK00553  245 KAKKVCVMATHGLFNKNAIQLFDEAFKKKLIdklfVSNSIPQTKFEKKPQFKVVDLAHLYEEVLLCYANGGSISAIY 321
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 11-127 4.52e-76

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 228.46  E-value: 4.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  11 MKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPVNLHLMELLIMIDACKRASAA 90
Cdd:pfam13793   1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPVNDNLMELLIMIDALKRASAK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1091062888  91 NINIVVPYYGYARQDRKARSREPITAKLVANLIETAG 127
Cdd:pfam13793  81 RITAVIPYFGYARQDRKDKPREPITAKLVADLLEAAG 117
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 12-307 1.74e-70

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 220.55  E-value: 1.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  12 KIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQpTSYPVNLHLMELLIMIDACKRASAAN 91
Cdd:PRK00934    1 MIIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGEIDGEDVVIIS-TTYPQDENLVELLLLIDALRDEGAKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  92 INIVVPYYGYARQDRKARSREPITAKLVANLIETAGaNRMIALDLHAPQIQGFFDIPIDHLMGVPILAQHFENDPDiNPe 171
Cdd:PRK00934   80 ITLVIPYLGYARQDKRFKPGEPISARAIAKIISAYY-DRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGDKLD-DP- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 172 ecVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAE--VMNIvgDIEGRTAIIIDDIIDTAGTITLAAQALKDKGA 249
Cdd:PRK00934  157 --LVLAPDKGALELAKEAAEILGCEYDYLEKTRISPTEVEiaPKNL--DVKGKDVLIVDDIISTGGTMATAIKILKEQGA 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1091062888 250 KEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLEENRkpnntkeLSVAGLIAKAI 307
Cdd:PRK00934  233 KKVYVACVHPVLVGDAILKLYNAGVDEIIVTDTLESEVSK-------ISVAPLIADLL 283
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 3-321 3.49e-44

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 155.11  E-value: 3.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   3 NNEYKNSSMKIFSLKGNEPLAQEVADH-VGIELG---------------------KCSVKRFSDGEIQINIEESIRGCDV 60
Cdd:PRK06827    1 METLPVGSLGIIALPSCRELADKVDEHlVRIRERkenenieslafkgysresyliPAKFIRFSNGEAKGEILESVRGKDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  61 FIVQP-TSYPV-------------NLHLMELLIMIDACkRASAANINIVVPYYGYARQDRKaRSREPITAKLVANLIETA 126
Cdd:PRK06827   81 YILQDvGNYSVtynmfgeknhmspDDHFQDLKRTIDAI-RGKARRITVIMPFLYESRQHKR-KGRESLDCALALQELEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 127 GANRMIALDLHAPQIQGFFdipidHLMGvpilaqhFEN----------------DPDINPEECVVVSPDHGGVTRARKLA 190
Cdd:PRK06827  159 GVDNIITFDAHDPRIENAI-----PLMG-------FENlypsyqiikallknekDLEIDKDHLMVISPDTGAMDRAKYYA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 191 DILKTPIAIIDKRRPKPNVAE-VMNIV------GDIEGRTAIIIDDIIDTAGTITLAAQALKDKGAKEVYACCTHPVL-S 262
Cdd:PRK06827  227 SVLGVDLGLFYKRRDYSRVVNgRNPIVaheflgRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAATFGFFtN 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091062888 263 GPAK--ERIENSAIKQLIVTNSI-QLEENRKPNNTKELSVAGLIAKAIIRVYERESVSVLFD 321
Cdd:PRK06827  307 GLEKfdKAYEEGYFDRIIGTNLVyHPEELLSKPWYIEVDMSKLIARIIDALNHDVSLSKLLD 368
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
9-310 2.56e-28

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 111.18  E-value: 2.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888   9 SSMKIFSLKGNEPLAQEVADHVGIELGKCSVKRFSDGEIQINIEESIRGCDVFIVQPTSYPvNLHLMELLIMIDACKRAS 88
Cdd:PRK07199    1 MQPLLLALPGNEAAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSLDRP-DEKLLPLLFAAEAARELG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  89 AANINIVVPYYGYARQDRKARSREPITAKLVANLIeTAGANRMIALD--LH-APQIQGFFDIPIDHLMGVPILAQHF-EN 164
Cdd:PRK07199   80 ARRVGLVAPYLAYMRQDIAFHPGEAISQRHFARLL-SGSFDRLVTVDphLHrYPSLSEVYPIPAVVLSAAPAIAAWIrAH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 165 DPDInpeecVVVSPDHGGVTRARKLADILKTPIAIIDKRR--------PKPNVAEvmnivgdIEGRTAIIIDDIIDTAGT 236
Cdd:PRK07199  159 VPRP-----LLIGPDEESEQWVAAVAERAGAPHAVLRKTRhgdrdveiSLPDAAP-------WAGRTPVLVDDIVSTGRT 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091062888 237 ITLAAQALKDKGAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIqleenrkPNNTKELSVAGLIAKAIIRV 310
Cdd:PRK07199  227 LIEAARQLRAAGAASPDCVVVHALFAGDAYSALAAAGIARVVSTDTV-------PHPSNAISLAPLLAEALRRE 293
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 174-320 2.14e-18

Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.


Pssm-ID: 434046  Cd Length: 184  Bit Score: 81.40  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 174 VVVSPDHGGVTRARKLADILKTPIAII------------DKRRPKPNVAEV------------------MNIVGDIEGRT 223
Cdd:pfam14572   6 VIVARSPGSAKRATSFAERLRLGIAVIhgeqkeaesdevDGRQSPPPYRSRtvsrslglpeiipkekppMTVVGDVGGRI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 224 AIIIDDIIDTAGTITLAAQALKDKGAKEVYACCTHPVLSGPAKERIENSAIKQLIVTNSIQLE-ENRKPNNTKELSVAGL 302
Cdd:pfam14572  86 AIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLLEASPIDEVVVTNTIPHEiQKMQCHKIKTIDISQL 165

                         170
                  ....*....|....*...
gi 1091062888 303 IAKAIIRVYERESVSVLF 320
Cdd:pfam14572 166 IAEAIRRIHNGESMSYLF 183
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 155-282 1.65e-15

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 72.04  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 155 VPILAQHFENDPDINPeecVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVM------NIVGDIEGRTAiiid 228
Cdd:cd06223     2 GRLLAEEIREDLLEPD---VVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEpyglelPLGGDVKGKRVllvd 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1091062888 229 diiDTAGTITLAAQALKDKGAKEVYACCTHPVLSGPAkeRIENSAIKQLIVTNS 282
Cdd:cd06223    79 dviATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA--RELASPGDPVYSLFT 130
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 20-307 9.76e-11

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 61.63  E-value: 9.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  20 EPLAQEVADHVG-IELGKCSVKRFSDG--EIQINIEESIRGCDV-FIVQPTSYPVnlhLMELLIMIDACKRASAANINIV 95
Cdd:PLN02297   26 EELARKIAAESDaIELGSINWRKFPDGfpNLFINNAHGIRGQHVaFLASFSSPAV---IFEQLSVIYALPKLFVASFTLV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888  96 VPYYGYARQDRKARSREPITA----KLVANL-IETAGANRMIALDLHAPQIQGFFDipiDHLM-----GVPILAQHFEND 165
Cdd:PLN02297  103 LPFFPTGTSERVEREGDVATAftlaRILSNIpISRGGPTSLVIFDIHALQERFYFG---DNVLpcfesGIPLLKKRLQQL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 166 PDinPEECVVVSPDHGGVTRARKLAD----ILKTPIAIIDKRrpkpnvaevmnIV----GDIEGRTAIIIDDIIDTAGTI 237
Cdd:PLN02297  180 PD--SDNIVIAFPDDGAWKRFHKQFEhfpmVVCTKVREGDKR-----------IVrikeGNPAGRHVVIVDDLVQSGGTL 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091062888 238 TLAAQALKDKGAKEVYACCTHPVLSGPAKERIENS------AIKQLIVTNSIQL--EENRKPNNTKELSVAGLIAKAI 307
Cdd:PLN02297  247 IECQKVLAAHGAAKVSAYVTHGVFPNESWERFTHDnggpeaGFAYFWITDSCPQtvKAVRGKAPFEVLSLAGSIADAL 324
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 157-268 1.23e-08

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 53.14  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091062888 157 ILAQHFENDPDINPeecVVVSPDHGGVTRARKLADILKTPIAIIDKRRPKPNVAEVM---NIVGDIEGRTAIIIDDIIDT 233
Cdd:pfam00156  18 LAAQINEDYGGKPD---VVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMktsSALPDLKGKTVLIVDDILDT 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1091062888 234 AGTITLAAQALKDKGAKEVYACCTHPVLSGPAKER 268
Cdd:pfam00156  95 GGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKD 129
 
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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