|
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: 784.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDILTAVHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 81 PEEWNAFVASASAGVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 241 LGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 544824516 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: 660.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDILTAVHKHYSP 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 82 EEWNAFVASASAGVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 162 GEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 544824516 322 SRLKELTKRTTFIRVQEQENRVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
3.00e-117 |
|
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: 342.19 E-value: 3.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 9 LGFKDVLIRPKRSTLkSRSDVELERQFTFKHSGQTwsgvPIIAANMDTVGTFEMATALAQFDILTAVHKHYSPEEWNAFV 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLNI----PLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 89 ASasagVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCE 166
Cdd:cd00381 77 RK----VKGRLLVgaAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 167 ELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 247 GHEESGGTVVEENGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKkgggdRYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 544824516 322 SRLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
3.16e-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: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 14 VLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDILTAVHKHYSPEEWNAFVASASA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 94 GVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHfvQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLgGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 254 TVVEENGEKFMLFYGMSSEsamtrhvggvAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 544824516 334 IRV 336
Cdd:COG0516 308 VRI 310
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
9-336 |
1.68e-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: 231.89 E-value: 1.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 9 LGFKDVLIRPKRSTLKSRsDVELERQFTFKHSGQtwsgVPIIAANMDTVGTFEMATALAQFDILTAVHKHYSPEEWNAFV 88
Cdd:pfam00478 2 LTFDDVLLVPGYSEVLPR-EVDLSTRLTRNITLN----IPLVSAAMDTVTEARMAIAMAREGGIGIIHKNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 89 A---SASAGV------------------------------------------------------VKHVM-------VSTG 104
Cdd:pfam00478 77 RkvkRSESGMitdpvtlspdatvadalalmerygisgvpvvddgklvgivtnrdlrfetdlsqpVSEVMtkenlvtAPEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 105 TS--DA----------------------------DFEKTKQILNAN-----------------------PAL-----NFV 126
Cdd:pfam00478 157 TTleEAkeilhkhkieklpvvddngrlvglitikDIEKAKEYPNAAkdeqgrlrvgaavgvgddtleraEALveagvDVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 127 CIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECA 206
Cdd:pfam00478 237 VVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVPQLTAIYDVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 207 DAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHV------G 280
Cdd:pfam00478 317 EAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLGAMKKGSkdryfqE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 544824516 281 GVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:pfam00478 397 DDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 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: 784.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDILTAVHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 81 PEEWNAFVASASAGVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 241 LGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 544824516 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: 660.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDILTAVHKHYSP 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 82 EEWNAFVASASAGVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 162 GEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 544824516 322 SRLKELTKRTTFIRVQEQENRVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
3.00e-117 |
|
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: 342.19 E-value: 3.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 9 LGFKDVLIRPKRSTLkSRSDVELERQFTFKHSGQTwsgvPIIAANMDTVGTFEMATALAQFDILTAVHKHYSPEEWNAFV 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLNI----PLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 89 ASasagVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCE 166
Cdd:cd00381 77 RK----VKGRLLVgaAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 167 ELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 247 GHEESGGTVVEENGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKkgggdRYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 544824516 322 SRLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
3.16e-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: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 14 VLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDILTAVHKHYSPEEWNAFVASASA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 94 GVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHfvQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLgGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 254 TVVEENGEKFMLFYGMSSEsamtrhvggvAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 544824516 334 IRV 336
Cdd:COG0516 308 VRI 310
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
9-336 |
1.68e-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: 231.89 E-value: 1.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 9 LGFKDVLIRPKRSTLKSRsDVELERQFTFKHSGQtwsgVPIIAANMDTVGTFEMATALAQFDILTAVHKHYSPEEWNAFV 88
Cdd:pfam00478 2 LTFDDVLLVPGYSEVLPR-EVDLSTRLTRNITLN----IPLVSAAMDTVTEARMAIAMAREGGIGIIHKNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 89 A---SASAGV------------------------------------------------------VKHVM-------VSTG 104
Cdd:pfam00478 77 RkvkRSESGMitdpvtlspdatvadalalmerygisgvpvvddgklvgivtnrdlrfetdlsqpVSEVMtkenlvtAPEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 105 TS--DA----------------------------DFEKTKQILNAN-----------------------PAL-----NFV 126
Cdd:pfam00478 157 TTleEAkeilhkhkieklpvvddngrlvglitikDIEKAKEYPNAAkdeqgrlrvgaavgvgddtleraEALveagvDVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 127 CIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECA 206
Cdd:pfam00478 237 VVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVPQLTAIYDVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 207 DAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHV------G 280
Cdd:pfam00478 317 EAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLGAMKKGSkdryfqE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 544824516 281 GVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:pfam00478 397 DDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 452
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
99-327 |
3.68e-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: 204.89 E-value: 3.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 99 VMVSTGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKV 178
Cdd:TIGR01302 215 VGAAVGTREFDKERAEALVKAG--VDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 179 GIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEE 258
Cdd:TIGR01302 293 GIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEII 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824516 259 NGEKFMLFYGMSSESAMTRhvGGVAKY---------RAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKEL 327
Cdd:TIGR01302 373 NGRRYKQYRGMGSLGAMTK--GSSDRYlqdenktkkFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
11-329 |
1.09e-57 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 189.78 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 11 FKDVLIRPKRSTLKSRSDVELERQF---TFKhsgqtwsgVPIIAANMDTVGTFEMATALAQFDILTAVHKhYSPEEWNAF 87
Cdd:PRK05458 7 YEDIQLIPNKCIVNSRSECDTSVTLgprTFK--------LPVVPANMQTIIDEKIAEWLAENGYFYIMHR-FDPEARIPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 88 V---------ASASAGVvkhvmvstgtSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGN 158
Cdd:PRK05458 78 IkdmheqgliASISVGV----------KDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 159 VVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYP--QLSAVIECADAAHglgGQIISDGGCTMPGDVAKAFGGGA 236
Cdd:PRK05458 148 VGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAAR---KPIIADGGIRTHGDIAKSIRFGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 237 DFVMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSEsamtrhvggVAK--YRAAEGKTVKLPLRGPVENTARDILGGLRS 314
Cdd:PRK05458 225 TMVMIGSLFAGHEESPGKTVEIDGKLYKEYFGSASE---------FQKgeYKNVEGKKILVPHKGSLKDTLTEMEQDLQS 295
|
330
....*....|....*
gi 544824516 315 ACTYVGASRLKELTK 329
Cdd:PRK05458 296 SISYAGGRDLDAIRK 310
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
97-337 |
5.84e-54 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 184.40 E-value: 5.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 97 KHVMV--STGTSDADFEKTKQILNAnpALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGAD 174
Cdd:PTZ00314 228 GQLLVgaAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGAD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 175 IVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGT 254
Cdd:PTZ00314 306 GLRIGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 255 VVEENGEKFMLFYGMSSESAM------TRHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELT 328
Cdd:PTZ00314 386 YFFKDGVRLKVYRGMGSLEAMlskesgERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELH 465
|
....*....
gi 544824516 329 KRTTFIRVQ 337
Cdd:PTZ00314 466 EKLYSGQVR 474
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
9-336 |
1.60e-51 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 176.00 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 9 LGFKDVLIRPKRSTLKSrSDVELERQFTFKHSgqtwSGVPIIAANMDTVGTFEMATALAQFDILTAVHKHYSPEE----- 83
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLTKNIS----LNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEAqrkei 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 84 -----WNAFVASASAGVVKHVMVSTGTSDADFEKTKQILNANPALNF--VC----------------------------- 127
Cdd:PRK06843 85 ekvktYKFQKTINTNGDTNEQKPEIFTAKQHLEKSDAYKNAEHKEDFpnACkdlnnklrvgaavsididtierveelvka 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 128 ------IDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSA 201
Cdd:PRK06843 165 hvdilvIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQITA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 202 VIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRhvGG 281
Cdd:PRK06843 245 ICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKR--GS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824516 282 VAKYRAAEGKTVK----------LPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:PRK06843 323 KSRYFQLENNEPKklvpegiegmVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVKI 387
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
128-330 |
1.88e-51 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 177.40 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 128 IDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECAD 207
Cdd:PRK07807 245 VDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLECAA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 208 AAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAG-HEESGGTVVEENGEKFMLFYGMSSESAM---TRHVGGVA 283
Cdd:PRK07807 325 AARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGtYESPGDLMRDRDGRPYKESFGMASARAVaarTAGDSAFD 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 544824516 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 |
2.22e-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: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 112 KTKQILNAnpALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVK 191
Cdd:TIGR01303 229 KAKALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMM 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 192 TGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVV-EENGEKFMLFYGMS 270
Cdd:TIGR01303 307 TGVGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMA 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544824516 271 SESAMTRHVGGVAKYRAA------EG-KTVKL---PLRGPVENTARDILGGLRSACTYVGASRLKELTKRTT 332
Cdd:TIGR01303 387 SKRAVVARTGADNAFDRArkalfeEGiSTSRMgldPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
99-290 |
1.54e-31 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 124.01 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 99 VMVSTGTSDADFEKTKQILNAnpALNFVCIDVANGYSEHFVQFVSKAREAWPTKTIIAGNVVTGEMCEELILSGADIVKV 178
Cdd:PLN02274 239 VGAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 179 GIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEE 258
Cdd:PLN02274 317 GMGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQ 396
|
170 180 190
....*....|....*....|....*....|....*..
gi 544824516 259 NGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEG 290
Cdd:PLN02274 397 DGVRVKKYRGMGSLEAMTkgsdqRYLGDTAKLKIAQG 433
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
97-336 |
2.94e-25 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 105.93 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 97 KHVMVSTGTSDADFEKTKqilnanPAL-----NFVCIDVANGYSEHFVQFVSKAREAWPTKTII-AGNVVTGEMCEELIL 170
Cdd:PRK07107 230 KRYVVGAGINTRDYAERV------PALveagaDVLCIDSSEGYSEWQKRTLDWIREKYGDSVKVgAGNVVDREGFRYLAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 171 SGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADA------AHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGM 244
Cdd:PRK07107 304 AGADFVKVGIGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIMLGRY 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 245 LAGHEESGGTVVEENGEKFMLFYGMSSESAMT---RHVGGVAKYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
Cdd:PRK07107 384 FARFDESPTNKVNINGNYMKEYWGEGSNRARNwqrYDLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGA 463
|
250
....*....|....*
gi 544824516 322 SRLKELTKRTTFIRV 336
Cdd:PRK07107 464 LSIPELQQKAKITLV 478
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
146-242 |
6.23e-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: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824516 146 REAWPTKTIIAGnVVTGEMCEELILSGADIVKV----GigpgsvctTRVKTGVgyPQLSAVIECADAAHGlGGQIISDGG 221
Cdd:COG1304 221 RERWPGPLIVKG-VLSPEDARRAVDAGVDGIDVsnhgG--------RQLDGGP--PTIDALPEIRAAVGG-RIPVIADGG 288
|
90 100
....*....|....*....|.
gi 544824516 222 CTMPGDVAKAFGGGADFVMLG 242
Cdd:COG1304 289 IRRGLDVAKALALGADAVGLG 309
|
|
| |
