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Conserved domains on  [gi|446354584|ref|WP_000432439|]
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MULTISPECIES: GMP reductase [Bacillus]

Protein Classification

guanosine monophosphate reductase( domain architecture ID 11481014)

Guanosine monophosphate reductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
 1-326 0e+00

guanosine 5'-monophosphate oxidoreductase; Provisional


:

Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 731.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   1 MENVFDYEDIQLIPAKCIVNSRSECDTTVTLGKHKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQPEKRISFIRD 80
Cdd:PRK05458   1 MMKVFDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFKLPVVPANMQTIIDEKIAEWLAENGYFYIMHRFDPEARIPFIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  81 MQSRGLIASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHA 160
Cdd:PRK05458  81 MHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 161 GADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAASKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESP 240
Cdd:PRK05458 161 GADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 241 GETIEKDGKLYKEYFGSASEFQKGEKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIRTVDYVVVKNSI 320
Cdd:PRK05458 241 GKTVEIDGKLYKEYFGSASEFQKGEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAIRKVDYVIVKNSI 320


                 ....*.
gi 446354584 321 FNGDKV 326
Cdd:PRK05458 321 FNGDKI 326
 
Name Accession Description Interval E-value
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
 1-326 0e+00

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 731.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   1 MENVFDYEDIQLIPAKCIVNSRSECDTTVTLGKHKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQPEKRISFIRD 80
Cdd:PRK05458   1 MMKVFDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFKLPVVPANMQTIIDEKIAEWLAENGYFYIMHRFDPEARIPFIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  81 MQSRGLIASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHA 160
Cdd:PRK05458  81 MHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 161 GADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAASKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESP 240
Cdd:PRK05458 161 GADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 241 GETIEKDGKLYKEYFGSASEFQKGEKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIRTVDYVVVKNSI 320
Cdd:PRK05458 241 GKTVEIDGKLYKEYFGSASEFQKGEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAIRKVDYVIVKNSI 320


                 ....*.
gi 446354584 321 FNGDKV 326
Cdd:PRK05458 321 FNGDKI 326
GMP_reduct_2 TIGR01306
guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP ...
 4-324 0e+00

guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP reductase. The other (TIGR01305) is found in eukaryotic and some proteobacterial lineages, including E. coli, while this family is found in a variety of bacterial lineages. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 130373  Cd Length: 321  Bit Score: 662.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584    4 VFDYEDIQLIPAKCIVNSRSECDTTVTLGKHKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQPEKRISFIRDMQS 83
Cdd:TIGR01306   1 VFDYEDIQLIPNKCIVNSRSECDTSVTLGKHKFKLPVVPANMQTIIDEKLAEQLAENGYFYIMHRFDEESRIPFIKDMQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   84 RGLIASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGAD 163
Cdd:TIGR01306  81 RGLFASISVGVKACEYEFVTQLAEEALTPEYITIDIAHGHSNSVINMIKHIKTHLPDSFVIAGNVGTPEAVRELENAGAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  164 ATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAASKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGET 243
Cdd:TIGR01306 161 ATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGASMVMIGSLFAGHEESPGET 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  244 IEKDGKLYKEYFGSASEFQKGEKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIRTVDYVVVKNSIFNG 323
Cdd:TIGR01306 241 VEKDGKLYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLSDTLIEMQQDLQSSISYAGGKDLDSLRTVDYVIVKNSIFNG 320


                  .
gi 446354584  324 D 324
Cdd:TIGR01306 321 D 321
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 5-316 4.65e-120

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: 348.35  E-value: 4.65e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   5 FDYEDIQLIPAKCIVnSRSECDTTVTLGK-HKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQ-PEKRISFIRDMQ 82
Cdd:cd00381    2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKnITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMsIEEQAEEVRKVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  83 SRgLIASISVGVKEDEYEFVQQLAAEqlSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGA 162
Cdd:cd00381   81 GR-LLVGAAVGTREDDKERAEALVEA--GVDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 163 DATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAASK---PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEES 239
Cdd:cd00381  158 DGVKVGIGPGSICTTRIVTGVGVP--QATAVADVAAAARDygvPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDES 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 240 PGETIEKDGKLYKEYFGSASEF--QKG----------EKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDA 307
Cdd:cd00381  236 PGEYIEINGKRYKEYRGMGSLGamKKGggdryfgeeaKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKE 315


                 ....*....
gi 446354584 308 IRTVDYVVV 316
Cdd:cd00381  316 LQEKARFVR 324
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 4-320 3.54e-96

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: 287.88  E-value: 3.54e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   4 VFDYEDIQLIPAKCIVNSRSECDTTVTLGKHKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQPEKRISFIRDMQS 83
Cdd:COG0516    2 VLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVDD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  84 RGLIASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSnaVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGAD 163
Cdd:COG0516   82 DGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHS--GGDAMKKIKLTFDDVLLIPGNSATVEPARALVDAGAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 164 ATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAASK--PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPG 241
Cdd:COG0516  160 LTKVGIGPGSICTTRVVIGLGIP--QLSAAMDTVTEARMaiAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446354584 242 ETIEKDGKLYKEYFGSASefqKGEKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIRTVDYVVVKNSI 320
Cdd:COG0516  238 EVILYQGRSVKRYRGMGS---DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRITSA 313
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 31-301 6.76e-69

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: 221.88  E-value: 6.76e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   31 LGKHKF-KLPVVpanmqtiiDEriatylaENNYFYIMHRFQPEKRISF---IRDMQSRgLIASISVGVKEDEYEFVQQLA 106
Cdd:pfam00478 166 LHKHKIeKLPVV--------DD-------NGRLVGLITIKDIEKAKEYpnaAKDEQGR-LRVGAAVGVGDDTLERAEALV 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  107 AEQLspEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGADATKVGIGPGKVCITKIKTGFGTG 186
Cdd:pfam00478 230 EAGV--DVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVP 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  187 gwQLAALRWCAKAASK---PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGETIEKDGKLYKEYFGSASE--- 260
Cdd:pfam00478 308 --QLTAIYDVAEAAKKygvPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLgam 385

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446354584  261 --------FQKGE-KKNV-EGKKMFVEHKGSLEDTLIEMEQDLQSSISYAG 301
Cdd:pfam00478 386 kkgskdryFQEDDdKKLVpEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCG 436
 
Name Accession Description Interval E-value
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
 1-326 0e+00

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 731.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   1 MENVFDYEDIQLIPAKCIVNSRSECDTTVTLGKHKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQPEKRISFIRD 80
Cdd:PRK05458   1 MMKVFDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFKLPVVPANMQTIIDEKIAEWLAENGYFYIMHRFDPEARIPFIKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  81 MQSRGLIASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHA 160
Cdd:PRK05458  81 MHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 161 GADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAASKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESP 240
Cdd:PRK05458 161 GADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 241 GETIEKDGKLYKEYFGSASEFQKGEKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIRTVDYVVVKNSI 320
Cdd:PRK05458 241 GKTVEIDGKLYKEYFGSASEFQKGEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAIRKVDYVIVKNSI 320


                 ....*.
gi 446354584 321 FNGDKV 326
Cdd:PRK05458 321 FNGDKI 326
GMP_reduct_2 TIGR01306
guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP ...
 4-324 0e+00

guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP reductase. The other (TIGR01305) is found in eukaryotic and some proteobacterial lineages, including E. coli, while this family is found in a variety of bacterial lineages. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 130373  Cd Length: 321  Bit Score: 662.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584    4 VFDYEDIQLIPAKCIVNSRSECDTTVTLGKHKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQPEKRISFIRDMQS 83
Cdd:TIGR01306   1 VFDYEDIQLIPNKCIVNSRSECDTSVTLGKHKFKLPVVPANMQTIIDEKLAEQLAENGYFYIMHRFDEESRIPFIKDMQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   84 RGLIASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGAD 163
Cdd:TIGR01306  81 RGLFASISVGVKACEYEFVTQLAEEALTPEYITIDIAHGHSNSVINMIKHIKTHLPDSFVIAGNVGTPEAVRELENAGAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  164 ATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAASKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGET 243
Cdd:TIGR01306 161 ATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGASMVMIGSLFAGHEESPGET 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  244 IEKDGKLYKEYFGSASEFQKGEKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIRTVDYVVVKNSIFNG 323
Cdd:TIGR01306 241 VEKDGKLYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLSDTLIEMQQDLQSSISYAGGKDLDSLRTVDYVIVKNSIFNG 320


                  .
gi 446354584  324 D 324
Cdd:TIGR01306 321 D 321
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 5-316 4.65e-120

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: 348.35  E-value: 4.65e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   5 FDYEDIQLIPAKCIVnSRSECDTTVTLGK-HKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQ-PEKRISFIRDMQ 82
Cdd:cd00381    2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKnITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMsIEEQAEEVRKVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  83 SRgLIASISVGVKEDEYEFVQQLAAEqlSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGA 162
Cdd:cd00381   81 GR-LLVGAAVGTREDDKERAEALVEA--GVDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 163 DATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAASK---PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEES 239
Cdd:cd00381  158 DGVKVGIGPGSICTTRIVTGVGVP--QATAVADVAAAARDygvPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDES 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 240 PGETIEKDGKLYKEYFGSASEF--QKG----------EKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDA 307
Cdd:cd00381  236 PGEYIEINGKRYKEYRGMGSLGamKKGggdryfgeeaKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKE 315


                 ....*....
gi 446354584 308 IRTVDYVVV 316
Cdd:cd00381  316 LQEKARFVR 324
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 4-320 3.54e-96

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: 287.88  E-value: 3.54e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   4 VFDYEDIQLIPAKCIVNSRSECDTTVTLGKHKFKLPVVPANMQTIIDERIATYLAENNYFYIMHRFQPEKRISFIRDMQS 83
Cdd:COG0516    2 VLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVDD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  84 RGLIASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSnaVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGAD 163
Cdd:COG0516   82 DGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHS--GGDAMKKIKLTFDDVLLIPGNSATVEPARALVDAGAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 164 ATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAASK--PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPG 241
Cdd:COG0516  160 LTKVGIGPGSICTTRVVIGLGIP--QLSAAMDTVTEARMaiAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446354584 242 ETIEKDGKLYKEYFGSASefqKGEKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIRTVDYVVVKNSI 320
Cdd:COG0516  238 EVILYQGRSVKRYRGMGS---DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRITSA 313
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 31-301 6.76e-69

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: 221.88  E-value: 6.76e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   31 LGKHKF-KLPVVpanmqtiiDEriatylaENNYFYIMHRFQPEKRISF---IRDMQSRgLIASISVGVKEDEYEFVQQLA 106
Cdd:pfam00478 166 LHKHKIeKLPVV--------DD-------NGRLVGLITIKDIEKAKEYpnaAKDEQGR-LRVGAAVGVGDDTLERAEALV 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  107 AEQLspEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGADATKVGIGPGKVCITKIKTGFGTG 186
Cdd:pfam00478 230 EAGV--DVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVP 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  187 gwQLAALRWCAKAASK---PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGETIEKDGKLYKEYFGSASE--- 260
Cdd:pfam00478 308 --QLTAIYDVAEAAKKygvPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLgam 385

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446354584  261 --------FQKGE-KKNV-EGKKMFVEHKGSLEDTLIEMEQDLQSSISYAG 301
Cdd:pfam00478 386 kkgskdryFQEDDdKKLVpEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCG 436
PRK05096 PRK05096
guanosine 5'-monophosphate oxidoreductase; Provisional
 6-322 1.25e-55

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235343 [Multi-domain]  Cd Length: 346  Bit Score: 184.38  E-value: 1.25e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   6 DYEDIQLIPAKCIVNSRSECDTTVTLgkhKFK--------LPVVPANMQTIIDERIATYLAENNYFYIMHRF-QPEKRIS 76
Cdd:PRK05096  10 GFKDVLIRPKRSTLKSRSDVELERQF---TFKhsgqswsgVPIIAANMDTVGTFEMAKALASFDILTAVHKHySVEEWAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  77 FIRDMQSRGL-IASISVGVKEDEYEFVQQLAAEQLSPEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVR 155
Cdd:PRK05096  87 FVNNSSADVLkHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVTGEMVE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 156 ELEHAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAA---SKPIIADGGIRTHGDVAKSIRFGATMVMVGSL 232
Cdd:PRK05096 167 ELILSGADIVKVGIGPGSVCTTRVKTGVGYP--QLSAVIECADAAhglGGQIVSDGGCTVPGDVAKAFGGGADFVMLGGM 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 233 FAGHEESPGETIEKDGKLYKEYFGSASEFqkGEKKNV---------EGKKMFVEHKGSLEDTLIEMEQDLQSSISYAGGT 303
Cdd:PRK05096 245 LAGHEESGGEIVEENGEKFMLFYGMSSES--AMKRHVggvaeyraaEGKTVKLPLRGPVENTARDILGGLRSACTYVGAS 322

                        330       340
                 ....*....|....*....|...
gi 446354584 304 KLDAI--RTVDYVVVK--NSIFN 322
Cdd:PRK05096 323 RLKELtkRTTFIRVQEqeNRVFN 345
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
 79-310 8.58e-55

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: 184.86  E-value: 8.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   79 RDMQSRgLIASISVGVKEDEYEFVQQLAAEQLspEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELE 158
Cdd:TIGR01302 207 KDENGR-LIVGAAVGTREFDKERAEALVKAGV--DVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALI 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  159 HAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAASK---PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAG 235
Cdd:TIGR01302 284 DAGADGLRVGIGPGSICTTRIVAGVGVP--QITAVYDVAEYAAQsgiPVIADGGIRYSGDIVKALAAGADAVMLGSLLAG 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  236 HEESPGETIEKDGKLYKEY--FGSASEFQKG------------EKKNVEGKKMFVEHKGSLEDTLIEMEQDLQSSISYAG 301
Cdd:TIGR01302 362 TTESPGEYEIINGRRYKQYrgMGSLGAMTKGssdrylqdenktKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVG 441


                  ....*....
gi 446354584  302 GTKLDAIRT 310
Cdd:TIGR01302 442 ARSIDELRE 450
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 86-313 1.95e-46

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 163.99  E-value: 1.95e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  86 LIASISVGVKEDEYEFVQQLAAEQLspEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGADAT 165
Cdd:PTZ00314 230 LLVGAAISTRPEDIERAAALIEAGV--DVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 166 KVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAASK---PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGE 242
Cdd:PTZ00314 308 RIGMGSGSICITQEVCAVGRP--QASAVYHVARYARErgvPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGE 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 243 TIEKDGKLYKEYFGSAS---EFQKGEKKN-------------VEGkkmFVEHKGSLEDTLIEMEQDLQSSISYAGGTKLD 306
Cdd:PTZ00314 386 YFFKDGVRLKVYRGMGSleaMLSKESGERyldenetikvaqgVSG---SVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIP 462


                 ....*..
gi 446354584 307 AIRTVDY 313
Cdd:PTZ00314 463 ELHEKLY 469
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
 7-309 1.64e-45

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 159.43  E-value: 1.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584   7 YEDIQLIPAKCIVNSrSECDTTVTLGKH-KFKLPVVPANMQTIIDERIATYLAENNYFYIMHR----------------F 69
Cdd:PRK06843  12 FDDVSLIPRKSSVLP-SEVSLKTQLTKNiSLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKnmsieaqrkeiekvktY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  70 QPEKRISF------------------------------------IRDMQSRgLIASISVGVKEDEYEFVQQLAAEQLspE 113
Cdd:PRK06843  91 KFQKTINTngdtneqkpeiftakqhleksdayknaehkedfpnaCKDLNNK-LRVGAAVSIDIDTIERVEELVKAHV--D 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 114 YITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGADATKVGIGPGKVCITKIKTGFGTGgwQLAAL 193
Cdd:PRK06843 168 ILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVP--QITAI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 194 rwC-----AKAASKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGETIEKDGKLYKEY--FGSASEFQKGEK 266
Cdd:PRK06843 246 --CdvyevCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYvgMGSISAMKRGSK 323

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446354584 267 ------KNVEGKKM-------FVEHKGSLEDTLIEMEQDLQSSISYAGGTKLDAIR 309
Cdd:PRK06843 324 sryfqlENNEPKKLvpegiegMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLK 379
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
115-306 2.46e-39

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 144.28  E-value: 2.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 115 ITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALR 194
Cdd:PRK07807 243 LVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRP--QFSAVL 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 195 WCAKAA---SKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGET-IEKDGKLYKEYFGSAS----------- 259
Cdd:PRK07807 321 ECAAAArelGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASaravaartagd 400

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446354584 260 -EFQKGEKKNVE----GKKMFV-EHKGSLEDTLIEMEQDLQSSISYAGGTKLD 306
Cdd:PRK07807 401 sAFDRARKALFEegisTSRMYLdPGRPGVEDLLDHITSGVRSSCTYAGARTLA 453
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 91-259 9.95e-32

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 124.01  E-value: 9.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  91 SVGVKEDEYEFVQQLAAEQLspEYITIDIAHGHSNAVINMIQHIKKHLPESFVIAGNVGTPEAVRELEHAGADATKVGIG 170
Cdd:PLN02274 242 AIGTRESDKERLEHLVKAGV--DVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMG 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 171 PGKVCITKIKTGFGTGgwQLAALRWCAKAASK---PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGETIEKD 247
Cdd:PLN02274 320 SGSICTTQEVCAVGRG--QATAVYKVASIAAQhgvPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQD 397

                        170
                 ....*....|..
gi 446354584 248 GKLYKEYFGSAS 259
Cdd:PLN02274 398 GVRVKKYRGMGS 409
PRK07107 PRK07107
IMP dehydrogenase;
117-286 1.50e-21

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 94.76  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 117 IDIAHGHSNAVINMIQHIKKHLPESFVI-AGNVGTPEAVRELEHAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRW 195
Cdd:PRK07107 260 IDSSEGYSEWQKRTLDWIREKYGDSVKVgAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIGRG--QATALIE 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 196 CAKAASK---------PIIADGGIRTHGDVAKSIRFGATMVMVGSLFAGHEESPGETIEKDGKLYKEYFGSAS----EFQ 262
Cdd:PRK07107 338 VAKARDEyfeetgvyiPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTNKVNINGNYMKEYWGEGSnrarNWQ 417

                        170       180       190
                 ....*....|....*....|....*....|
gi 446354584 263 K----GEKKNV--EGKKMFVEHKGSLEDTL 286
Cdd:PRK07107 418 RydlgGDKKLSfeEGVDSYVPYAGSLKDNV 447
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 150-230 3.99e-08

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: 53.98  E-value: 3.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 150 TPEAVRELEHAGADATKVGigpgkvcitkiktgfGTGGWQL-------AALRWCAKAASK--PIIADGGIRTHGDVAKSI 220
Cdd:COG1304  235 SPEDARRAVDAGVDGIDVS---------------NHGGRQLdggpptiDALPEIRAAVGGriPVIADGGIRRGLDVAKAL 299

                         90
                 ....*....|
gi 446354584 221 RFGATMVMVG 230
Cdd:COG1304  300 ALGADAVGLG 309
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 131-231 1.63e-07

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.


Pssm-ID: 426849 [Multi-domain]  Cd Length: 180  Bit Score: 50.62  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  131 IQHIKKHLPESFVIAGNVGTPEAVRELEHAGADAtkVGIGPgkVCITKIKTGFGTGGWQLaaLRWCAKAASKPIIADGGI 210
Cdd:pfam02581  85 VAEARELLGPDLIIGVSTHTLEEALEAEALGADY--IGFGP--IFPTPTKPDAPPLGLEG--LKAIAEAVEIPVVAIGGI 158

                          90       100
                  ....*....|....*....|.
gi 446354584  211 RTHgDVAKSIRFGATMVMVGS 231
Cdd:pfam02581 159 TPE-NVPEVIEAGADGVAVVS 178
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 131-237 5.94e-07

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 49.05  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 131 IQHIKKHLPESFVIAGNVGTPEAVRELEHAGADAtkVGIGPgkvcI--TKIKTGFGTGgWQLAALRWCAKAASKPIIADG 208
Cdd:cd00564   85 VAEARALLGPDLIIGVSTHSLEEALRAEELGADY--VGFGP----VfpTPTKPGAGPP-LGLELLREIAELVEIPVVAIG 157

                         90       100
                 ....*....|....*....|....*....
gi 446354584 209 GIrTHGDVAKSIRFGATMVMVGSLFAGHE 237
Cdd:cd00564  158 GI-TPENAAEVLAAGADGVAVISAITGAD 185
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 134-246 7.65e-07

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 50.20  E-value: 7.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  134 IKKHLPESFVIAGnVGTPEAVRELEHAGADATKVGIGPGKVCITKIKTGfGTGGWQLAALrwCAKAASKPIIADGGIRTH 213
Cdd:pfam03060 130 FRLHFAGVALIPT-ISSAKEARIAEARGADALIVQGPEAGGHQGTPEYG-DKGLFRLVPQ--VPDAVDIPVIAAGGIWDR 205

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446354584  214 GDVAKSIRFGATMVMVGSLFAGHEESPGETIEK 246
Cdd:pfam03060 206 RGVAAALALGASGVQMGTRFLLTKESGAHDAHK 238
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 148-240 8.41e-07

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 49.40  E-value: 8.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 148 VGTPEAVRELEHAGADAtkvgigpgkVCITKIKTGfGTGGWQLAA----LRWCAKAASKPIIADGGIRTHGDVAKSIRFG 223
Cdd:cd04730  109 VTSVEEARKAEAAGADA---------LVAQGAEAG-GHRGTFDIGtfalVPEVRDAVDIPVIAAGGIADGRGIAAALALG 178

                         90
                 ....*....|....*..
gi 446354584 224 ATMVMVGSLFAGHEESP 240
Cdd:cd04730  179 ADGVQMGTRFLATEESG 195
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 106-231 2.63e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 47.20  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 106 AAEQLSPEYITIDIAHGHSNA-VINMIQHIKKHLPE-SFVIAGNVGTPEAVRELEHAGADATKVGIGPGkvcITKIKTGF 183
Cdd:cd04722   79 AARAAGADGVEIHGAVGYLAReDLELIRELREAVPDvKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGG---GGGGRDAV 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446354584 184 GTGGWQLAALRwcaKAASKPIIADGGIRTHGDVAKSIRFGATMVMVGS 231
Cdd:cd04722  156 PIADLLLILAK---RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 130-246 3.94e-06

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 46.72  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 130 MIQHIKKHLPESFVIAGNVGTPEAVRELEHAGADAtkVGIGPgkVCITKIKTGFGTGgWQLAALRWCAKAASKPIIADGG 209
Cdd:COG0352   89 PVAEARALLGPDLIIGVSCHSLEEALRAEEAGADY--VGFGP--VFPTPTKPGAPPP-LGLEGLAWWAELVEIPVVAIGG 163

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446354584 210 IrTHGDVAKSIRFGATMVMVGSLFAGHEEsPGETIEK 246
Cdd:COG0352  164 I-TPENAAEVLAAGADGVAVISAIWGAPD-PAAAARE 198
FMN_dh pfam01070
FMN-dependent dehydrogenase;
186-238 1.28e-05

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 46.37  E-value: 1.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446354584  186 GGWQL-------AALRWCAKAASK--PIIADGGIRTHGDVAKSIRFGATMVMVG-----SLFAGHEE 238
Cdd:pfam01070 249 GGRQLdgapatiDALPEIVAAVGGriPVLVDGGIRRGTDVLKALALGADAVLLGrpflyGLAAGGEA 315
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 127-246 9.50e-05

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 43.64  E-value: 9.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 127 VINMIQHIKKHL--PesfVIAGNVG---TPEAVRELEHAGADATKVGigpgkvcitkiktgfGTGG--WQL--------- 190
Cdd:cd02811  166 WLERIEELVKALsvP---VIVKEVGfgiSRETAKRLADAGVKAIDVA---------------GAGGtsWARvenyrakds 227

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446354584 191 ----------------AALRWCAKAASK-PIIADGGIRTHGDVAKSIRFGATMV-MVGSLFAGHEESPGETIEK 246
Cdd:cd02811  228 dqrlaeyfadwgiptaASLLEVRSALPDlPLIASGGIRNGLDIAKALALGADLVgMAGPFLKAALEGEEAVIET 301
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 186-230 1.41e-04

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 43.28  E-value: 1.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446354584 186 GGWQLA-------ALRWCAKAASKPIIADGGIRTHGDVAKSIRFGATMVMVG 230
Cdd:cd04736  267 GGRQLDdaiapieALAEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLG 318
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 86-231 1.74e-04

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 42.73  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584  86 LIASIsVGVKEDEYEFVQQLAAEQLSPeYITIDI-----AHGHSN-----AVINMIQHIKKHLPESFVI--AGNVGT--- 150
Cdd:cd02810  101 LIASV-GGSSKEDYVELARKIERAGAK-ALELNLscpnvGGGRQLgqdpeAVANLLKAVKAAVDIPLLVklSPYFDLedi 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 151 PEAVRELEHAGADAT------------KVGIGPGKVCITkiktgFGTGGWQL--AALRWCAKAAS-----KPIIADGGIR 211
Cdd:cd02810  179 VELAKAAERAGADGLtaintisgrvvdLKTVGPGPKRGT-----GGLSGAPIrpLALRWVARLAArlqldIPIIGVGGID 253

                        170       180
                 ....*....|....*....|
gi 446354584 212 THGDVAKSIRFGATMVMVGS 231
Cdd:cd02810  254 SGEDVLEMLMAGASAVQVAT 273
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 186-230 2.45e-04

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 42.05  E-value: 2.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446354584 186 GGWQL-------AALRWCAKAASK--PIIADGGIRTHGDVAKSIRFGATMVMVG 230
Cdd:cd02809  203 GGRQLdgapatiDALPEIVAAVGGriEVLLDGGIRRGTDVLKALALGADAVLIG 256
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 129-231 5.85e-04

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 40.64  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 129 NMIQHIKKHLpESFVIAgNVGTPEAVRELEHAGADAtkvgIGPGKVCITKIKTGFGTGGWQLaaLRWCAKAASKPIIADG 208
Cdd:cd04729  113 ELIKRIHEEY-NCLLMA-DISTLEEALNAAKLGFDI----IGTTLSGYTEETAKTEDPDFEL--LKELRKALGIPVIAEG 184

                         90       100
                 ....*....|....*....|...
gi 446354584 209 GIRTHGDVAKSIRFGATMVMVGS 231
Cdd:cd04729  185 RINSPEQAAKALELGADAVVVGS 207
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 152-230 6.30e-04

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 41.02  E-value: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 152 EAVRELEHAGADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAASKPIIADGGIRThGDVAKSI--RFGATMVMV 229
Cdd:cd02803  232 EIAKALEEAGVDALHVSGGSYESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRD-PEVAEEIlaEGKADLVAL 310


                 .
gi 446354584 230 G 230
Cdd:cd02803  311 G 311
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 148-240 1.34e-03

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 39.71  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 148 VGTPEAVRELEHAGADAtkvgigpgkVCITkiktGFGTGG----WQL---AALRWCAKAASKPIIADGGIRTHGDVAKSI 220
Cdd:COG2070  111 VTSVREARKAEKAGADA---------VVAE----GAEAGGhrgaDEVstfALVPEVRDAVDIPVIAAGGIADGRGIAAAL 177

                         90       100
                 ....*....|....*....|
gi 446354584 221 RFGATMVMVGSLFAGHEESP 240
Cdd:COG2070  178 ALGADGVQMGTRFLATEESP 197
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 101-230 1.45e-03

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 40.12  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 101 FVQQLAAEQLSPEyitiDIahghsnavinmiQHIKKH--LPesfVIAGNVGTPEAVRELEHAGADATKVGIGPGKvcitK 178
Cdd:cd04737  199 EIYAAAKQKLSPA----DI------------EFIAKIsgLP---VIVKGIQSPEDADVAINAGADGIWVSNHGGR----Q 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446354584 179 IKTGFGTggwqLAALRWCAKAASK--PIIADGGIRTHGDVAKSIRFGATMVMVG 230
Cdd:cd04737  256 LDGGPAS----FDSLPEIAEAVNHrvPIIFDSGVRRGEHVFKALASGADAVAVG 305
thiE PRK00043
thiamine phosphate synthase;
138-229 4.23e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 37.85  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 138 LPESFVIAGNVGTPEAVRELEHAGADAtkVGIGPgkVCITKIKTGfGTGGWQLAALR-WCAKAASKPIIADGGIrTHGDV 216
Cdd:PRK00043 101 LGPDAIIGLSTHTLEEAAAALAAGADY--VGVGP--IFPTPTKKD-AKAPQGLEGLReIRAAVGDIPIVAIGGI-TPENA 174

                         90
                 ....*....|...
gi 446354584 217 AKSIRFGATMVMV 229
Cdd:PRK00043 175 PEVLEAGADGVAV 187
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 158-231 6.29e-03

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 37.91  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354584 158 EHAGADAtkvgigpgkvcITKIKT---------------GFGTGGwqLA-------ALR--W-CAKAASKPIIADGGIRT 212
Cdd:cd04740  176 EEAGADG-----------LTLINTlkgmaidietrkpilGNVTGG--LSgpaikpiALRmvYqVYKAVEIPIIGVGGIAS 242

                         90
                 ....*....|....*....
gi 446354584 213 HGDVAKSIRFGATMVMVGS 231
Cdd:cd04740  243 GEDALEFLMAGASAVQVGT 261
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 201-246 6.95e-03

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 37.63  E-value: 6.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446354584 201 SKPIIADGGIRTHGDVAKSIRFGATMVMVGSLFagHEESPG--ETIEK 246
Cdd:PRK02506 241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTAL--HKEGPAvfERLTK 286
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 190-233 7.01e-03

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 37.74  E-value: 7.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446354584 190 LAALRWCAKAASK--PIIADGGIRTHGDVAKSIRFGATMVMVGSLF 233
Cdd:COG0167  223 LRMVREVAQAVGGdiPIIGVGGISTAEDALEFILAGASAVQVGTAL 268
 
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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