|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-346 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 784.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFGMATALAQFDILTAVHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 81 PEEWNAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 241 LGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 1738280109 321 ASRLKELTKRTTFIRVQEQENRVFNS 346
Cdd:PRK05096 321 ASRLKELTKRTTFIRVQEQENRVFNN 346
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
2-344 |
0e+00 |
|
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP reductase. This family includes both eukaryotic and some proteobacterial sequences, while the other family contains other bacterial sequences. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 130372 Cd Length: 343 Bit Score: 660.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFGMATALAQFDILTAVHKHYSP 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 82 EEWNAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 162 GEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 1738280109 322 SRLKELTKRTTFIRVQEQENRVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.09e-116 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 339.88 E-value: 2.09e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 9 LGFKDVLIRPKRSTLkSRSDVELERQFTFKHSGQTwsgvPIIAANMDTVGTFGMATALAQFDILTAVHKHYSPEEWNAFV 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLNI----PLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 89 AsasaDVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCE 166
Cdd:cd00381 77 R----KVKGRLLVgaAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 167 ELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 247 GHEESGGTVVEENGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKkgggdRYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 1738280109 322 SRLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
3.19e-84 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 257.83 E-value: 3.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 14 VLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFGMATALAQFDILTAVHKHYSPEEWNAFVASASA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 94 DVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHfvQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLgGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 254 TVVEENGEKFMLFYGMSSEsamtrhvggvAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 1738280109 334 IRV 336
Cdd:COG0516 308 VRI 310
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
104-336 |
2.99e-72 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 231.51 E-value: 2.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 104 GTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPG 183
Cdd:pfam00478 216 GVGDDTLERAEALVEAG--VDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 184 SVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKF 263
Cdd:pfam00478 294 SICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRY 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1738280109 264 MLFYGMSSESAMTRHV------GGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:pfam00478 374 KSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 452
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-346 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 784.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFGMATALAQFDILTAVHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 81 PEEWNAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 241 LGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 1738280109 321 ASRLKELTKRTTFIRVQEQENRVFNS 346
Cdd:PRK05096 321 ASRLKELTKRTTFIRVQEQENRVFNN 346
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
2-344 |
0e+00 |
|
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP reductase. This family includes both eukaryotic and some proteobacterial sequences, while the other family contains other bacterial sequences. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 130372 Cd Length: 343 Bit Score: 660.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFGMATALAQFDILTAVHKHYSP 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 82 EEWNAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 162 GEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 1738280109 322 SRLKELTKRTTFIRVQEQENRVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.09e-116 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 339.88 E-value: 2.09e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 9 LGFKDVLIRPKRSTLkSRSDVELERQFTFKHSGQTwsgvPIIAANMDTVGTFGMATALAQFDILTAVHKHYSPEEWNAFV 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLNI----PLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 89 AsasaDVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCE 166
Cdd:cd00381 77 R----KVKGRLLVgaAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 167 ELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 247 GHEESGGTVVEENGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKkgggdRYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 1738280109 322 SRLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
3.19e-84 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 257.83 E-value: 3.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 14 VLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFGMATALAQFDILTAVHKHYSPEEWNAFVASASA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 94 DVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHfvQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLgGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 254 TVVEENGEKFMLFYGMSSEsamtrhvggvAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 1738280109 334 IRV 336
Cdd:COG0516 308 VRI 310
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
104-336 |
2.99e-72 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 231.51 E-value: 2.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 104 GTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPG 183
Cdd:pfam00478 216 GVGDDTLERAEALVEAG--VDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 184 SVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKF 263
Cdd:pfam00478 294 SICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRY 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1738280109 264 MLFYGMSSESAMTRHV------GGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:pfam00478 374 KSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 452
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
90-327 |
1.49e-62 |
|
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273546 [Multi-domain] Cd Length: 450 Bit Score: 206.04 E-value: 1.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 90 SASADVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEE 167
Cdd:TIGR01302 204 HASKDENGRLIVgaAVGTREFDKERAEALVKAG--VDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 168 LILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAG 247
Cdd:TIGR01302 282 LIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAG 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 248 HEESGGTVVEENGEKFMLFYGMSSESAMTRhvGGVAKY---------RAAEGKTVKLPLRGPVENTARDILGGLRSACTY 318
Cdd:TIGR01302 362 TTESPGEYEIINGRRYKQYRGMGSLGAMTK--GSSDRYlqdenktkkFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGY 439
|
....*....
gi 1738280109 319 VGASRLKEL 327
Cdd:TIGR01302 440 VGARSIDEL 448
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
11-329 |
2.39e-56 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 186.31 E-value: 2.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 11 FKDVLIRPKRSTLKSRSDVELERQF---TFKhsgqtwsgVPIIAANMDTVGTFGMATALAQFDILTAVHKhYSPEEWNAF 87
Cdd:PRK05458 7 YEDIQLIPNKCIVNSRSECDTSVTLgprTFK--------LPVVPANMQTIIDEKIAEWLAENGYFYIMHR-FDPEARIPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 88 VAS-------ASadvvkhvmVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVV 160
Cdd:PRK05458 78 IKDmheqgliAS--------ISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYP--QLSAVIECADAAHglgGQIISDGGCTMPGDVAKAFGGGADF 238
Cdd:PRK05458 150 TPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAAR---KPIIADGGIRTHGDIAKSIRFGATM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 239 VMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSEsamtrhvggVAK--YRAAEGKTVKLPLRGPVENTARDILGGLRSAC 316
Cdd:PRK05458 227 VMIGSLFAGHEESPGKTVEIDGKLYKEYFGSASE---------FQKgeYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSI 297
|
330
....*....|...
gi 1738280109 317 TYVGASRLKELTK 329
Cdd:PRK05458 298 SYAGGRDLDAIRK 310
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
91-337 |
5.18e-55 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 187.10 E-value: 5.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 91 ASADVVKHVMV--STGTSDADFEKTKQILNAnpALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEEL 168
Cdd:PTZ00314 222 ASLDSNGQLLVgaAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 169 ILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGH 248
Cdd:PTZ00314 300 IDAGADGLRIGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGT 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 249 EESGGTVVEENGEKFMLFYGMSSESAM------TRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGAS 322
Cdd:PTZ00314 380 EEAPGEYFFKDGVRLKVYRGMGSLEAMlskesgERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAH 459
|
250
....*....|....*
gi 1738280109 323 RLKELTKRTTFIRVQ 337
Cdd:PTZ00314 460 SIPELHEKLYSGQVR 474
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
9-336 |
4.37e-52 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 177.54 E-value: 4.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 9 LGFKDVLIRPKRSTLKSrSDVELERQFTFKHSgqtwSGVPIIAANMDTVGTFGMATALAQFDILTAVHKHYSPE------ 82
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLTKNIS----LNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEaqrkei 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 83 -----------------------------------------EWNAFVASASADVVKHVMVSTGTS-DAD-FEKTKQILNA 119
Cdd:PRK06843 85 ekvktykfqktintngdtneqkpeiftakqhleksdayknaEHKEDFPNACKDLNNKLRVGAAVSiDIDtIERVEELVKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 120 NpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQL 199
Cdd:PRK06843 165 H--VDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 200 SAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRhv 279
Cdd:PRK06843 243 TAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKR-- 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1738280109 280 GGVAKYRAAEGKTVK----------LPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:PRK06843 321 GSKSRYFQLENNEPKklvpegiegmVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVKI 387
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
128-330 |
2.04e-51 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 177.40 E-value: 2.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 128 IDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECAD 207
Cdd:PRK07807 245 VDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLECAA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 208 AAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAG-HEESGGTVVEENGEKFMLFYGMSSESAM---TRHVGGVA 283
Cdd:PRK07807 325 AARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGtYESPGDLMRDRDGRPYKESFGMASARAVaarTAGDSAFD 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1738280109 284 KYRAA---EG-KTVKL---PLRGPVENTARDILGGLRSACTYVGASRLKELTKR 330
Cdd:PRK07807 405 RARKAlfeEGiSTSRMyldPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHER 458
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
112-332 |
2.44e-49 |
|
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase and restricted to the high GC Gram-positive bacteria. All species in which a member is found so far (Corynebacterium glutamicum, Mycobacterium tuberculosis, Streptomyces coelicolor, etc.) also have IMP dehydrogenase as described by TIGRFAMs entry TIGR01302. [Unknown function, General]
Pssm-ID: 130370 [Multi-domain] Cd Length: 475 Bit Score: 172.02 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 112 KTKQILNAnpALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVK 191
Cdd:TIGR01303 229 KAKALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMM 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 192 TGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVV-EENGEKFMLFYGMS 270
Cdd:TIGR01303 307 TGVGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMA 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1738280109 271 SESAMTRHVGGVAKYRAA------EG-KTVKL---PLRGPVENTARDILGGLRSACTYVGASRLKELTKRTT 332
Cdd:TIGR01303 387 SKRAVVARTGADNAFDRArkalfeEGiSTSRMgldPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
99-290 |
1.52e-31 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 124.01 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 99 VMVSTGTSDADFEKTKQILNAnpALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKV 178
Cdd:PLN02274 239 VGAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 179 GIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEE 258
Cdd:PLN02274 317 GMGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQ 396
|
170 180 190
....*....|....*....|....*....|....*..
gi 1738280109 259 NGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEG 290
Cdd:PLN02274 397 DGVRVKKYRGMGSLEAMTkgsdqRYLGDTAKLKIAQG 433
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
94-336 |
2.99e-25 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 105.93 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 94 DVVKHVMVSTGTSDADFEKTKqilnanPAL-----NFVCIDVANGYSEHFVQFVSKAREAWPTKTII-AGNVVTGEMCEE 167
Cdd:PRK07107 227 DSSKRYVVGAGINTRDYAERV------PALveagaDVLCIDSSEGYSEWQKRTLDWIREKYGDSVKVgAGNVVDREGFRY 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 168 LILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADA------AHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:PRK07107 301 LAEAGADFVKVGIGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIML 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMT---RHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTY 318
Cdd:PRK07107 381 GRYFARFDESPTNKVNINGNYMKEYWGEGSNRARNwqrYDLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCN 460
|
250
....*....|....*...
gi 1738280109 319 VGASRLKELTKRTTFIRV 336
Cdd:PRK07107 461 CGALSIPELQQKAKITLV 478
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
146-242 |
6.63e-03 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 38.19 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738280109 146 REAWPTKTIIAGnVVTGEMCEELILSGADIVKV----GigpgsvctTRVKTGVgyPQLSAVIECADAAHGlGGQIISDGG 221
Cdd:COG1304 221 RERWPGPLIVKG-VLSPEDARRAVDAGVDGIDVsnhgG--------RQLDGGP--PTIDALPEIRAAVGG-RIPVIADGG 288
|
90 100
....*....|....*....|.
gi 1738280109 222 CTMPGDVAKAFGGGADFVMLG 242
Cdd:COG1304 289 IRRGLDVAKALALGADAVGLG 309
|
|
| |
