|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
1-396 |
0e+00 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 661.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 1 MFLIGEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFG 80
Cdd:PRK13307 1 MYLIGEALIGEGNELAHIDLIIGDKEGPVGQAFANGLTQLSAGHTPLLAVIRPNLITKPATLIVPKVTVKNMEQAELIFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 81 PAQNAVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHP 160
Cdd:PRK13307 81 PAQAAVAKAVADAVEEGIIPKDKAEDLVIVASVFIHPTAKDYNKIYQYNYGATKLAIKRALEGFPDVDKVLYEKDRALHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 161 IMGFRVIRLWDPPYLQVALDLVDLTVVRRVLSQLPDSDHLLIEVGTPLVKKFGASVVKEIRNVRPSSFVVLDLKTLDTGN 240
Cdd:PRK13307 161 IMGFKVTRLWDPPYLQVALDLPDLEEVERVLSQLPKSDHIIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 241 LEVRLAADATADAVVISGLAPQKTLELAIREARKTGIYSVIDMLNVPDPLEVLRSLAVLPDVVEMHRAIDQEAERHNWEA 320
Cdd:PRK13307 241 LEARMAADATADAVVISGLAPISTIEKAIHEAQKTGIYSILDMLNVEDPVKLLESLKVKPDVVELHRGIDEEGTEHAWGN 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504398499 321 IAEIKRMaassDRKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELKQtEIDQYRVMTDF 396
Cdd:PRK13307 321 IKEIKKA----GGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKLKP-DIDQFRLMTDF 391
|
|
| Fae |
COG1795 |
Formaldehyde-activating enzyme (5,6,7,8-tetrahydromethanopterin hydrolyase) [Energy production ... |
1-166 |
3.14e-104 |
|
Formaldehyde-activating enzyme (5,6,7,8-tetrahydromethanopterin hydrolyase) [Energy production and conversion];
Pssm-ID: 441400 Cd Length: 171 Bit Score: 304.83 E-value: 3.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 1 MFLIGEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFG 80
Cdd:COG1795 5 MMLIGEALVGDGNEVAHIDLIIGPRDGPVGTAFANALANQSAGHTPLLAVLAPNLPVKPATLMVPKVTIKNAKQANQMFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 81 PAQNAVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHP 160
Cdd:COG1795 85 PAQAAVAKAVADAVAEGVIPKDEADDLVIIVSVFIHPEADDDKKIYRYNYEATKLAIKRAMAGEPSIDEVLANKDRAKHP 164
|
....*.
gi 504398499 161 IMGFRV 166
Cdd:COG1795 165 FAGFKV 170
|
|
| one_C_fae |
TIGR03126 |
formaldehyde-activating enzyme; This family consists of formaldehyde-activating enzyme, or the ... |
2-161 |
2.34e-99 |
|
formaldehyde-activating enzyme; This family consists of formaldehyde-activating enzyme, or the corresponding domain of longer, bifunctional proteins. It links formaldehyde to the C1 carrier tetrahydromethanopterin (H4MPT), an analog of tetrahydrofolate, and is common among species with H4MPT. The ribulose monophosphate (RuMP) pathway, which removes the toxic metabolite formaldehyde by assimilation, runs in the opposite direction in some species to produce ribulose 5-phosphate for nucleotide biosynthesis, leaving formaldehyde as an additional metabolite. In these species, formaldehyde activating enzyme may occur as a fusion protein with D-arabino 3-hexulose 6-phosphate formaldehyde lyase from the RuMP pathway.
Pssm-ID: 132170 Cd Length: 160 Bit Score: 292.33 E-value: 2.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 2 FLIGEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFGP 81
Cdd:TIGR03126 1 YRIGEALIGEGNEVAHIDLIIGPKGGPVGTAFANALANLSAGHTPLLAVLRPNLPTKPATLIVPKVTIKNMAQAVQMFGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 82 AQNAVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHPI 161
Cdd:TIGR03126 81 AQAAVAKAVADSVEEGIIPKDEADDLVIIVSVFIHPEAKDDRKIYKYNYEATKLAIKRAMEGEPSVDEVLAKKDSATHPF 160
|
|
| Fae |
pfam08714 |
Formaldehyde-activating enzyme (Fae); Formaldehyde-activating enzyme is an enzyme required for ... |
5-162 |
5.81e-98 |
|
Formaldehyde-activating enzyme (Fae); Formaldehyde-activating enzyme is an enzyme required for energy metabolism and formaldehyde detoxification. It catalyzes the condensation of formaldehyde and tetrahydromethanopterin to methylene tetrahydromethanopterin.
Pssm-ID: 430170 Cd Length: 158 Bit Score: 288.69 E-value: 5.81e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 5 GEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFGPAQN 84
Cdd:pfam08714 1 GEALVGEGNEVAHIDLIIGPKGGPVGTAFANALTNQSAGHTPLLAVLRPNLMVKPATLMVPKVTIKNMKQAELMFGPAQA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504398499 85 AVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHPIM 162
Cdd:pfam08714 81 AVAKAVADAVEEGIIPKDEADDLVIIVSVFIHPDALDKRKIYRYNYEATKLAIKRAMAGEPSIDEVLAEKDRAKHPFM 158
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
173-378 |
3.76e-64 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 203.58 E-value: 3.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 173 PYLQVALDLVDLTVVRRVLSQLPDSdHLLIEVGTPLVKKFGASVVKEIRNVRPSSFVVLDLKTLDTGNLEVRLAADATAD 252
Cdd:cd04726 1 PLLQVALDLLDLEEALELAKKVPDG-VDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 253 AVVISGLAPQKTLELAIREARKTGIYSVIDMLNVPDPLEVLRSLAVLPDVVEMHRAIDQEAERhNWEAIAEIKRMaaSSD 332
Cdd:cd04726 80 IVTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAG-GWWPEDDLKKV--KKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504398499 333 RKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:cd04726 157 LGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| OMPdecase |
smart00934 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ... |
174-378 |
1.35e-29 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 113.80 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 174 YLQVALDLVDLTVVRRVLSQLPDSdHLLIEVGTPLVKKFGASVVKEIRNVRPSsFVVLDLKTLDTGNLEVRLAADATADA 253
Cdd:smart00934 1 RLIVALDVPDLEEALELADALGDS-VDIIKVGTELFLAEGPEGVKELKELFGF-PVFLDLKLHDIPNTVARAARAAAELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 254 VV---ISGLAPQKTLELAIREARKTG-IYSVIDMLNVPDPLEV--------------LRSLAVLPDVVEMHRAIDQeaer 315
Cdd:smart00934 79 ADavtVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLqelgdesleeqvlrLAKLAKEAGLDGVVCSATE---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504398499 316 hnweaiAEIKRMAASSDRKVLVAvagGI----RVDTVASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:smart00934 155 ------PELIRRALGPDFLILTP---GIgdqgRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
1-396 |
0e+00 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 661.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 1 MFLIGEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFG 80
Cdd:PRK13307 1 MYLIGEALIGEGNELAHIDLIIGDKEGPVGQAFANGLTQLSAGHTPLLAVIRPNLITKPATLIVPKVTVKNMEQAELIFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 81 PAQNAVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHP 160
Cdd:PRK13307 81 PAQAAVAKAVADAVEEGIIPKDKAEDLVIVASVFIHPTAKDYNKIYQYNYGATKLAIKRALEGFPDVDKVLYEKDRALHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 161 IMGFRVIRLWDPPYLQVALDLVDLTVVRRVLSQLPDSDHLLIEVGTPLVKKFGASVVKEIRNVRPSSFVVLDLKTLDTGN 240
Cdd:PRK13307 161 IMGFKVTRLWDPPYLQVALDLPDLEEVERVLSQLPKSDHIIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 241 LEVRLAADATADAVVISGLAPQKTLELAIREARKTGIYSVIDMLNVPDPLEVLRSLAVLPDVVEMHRAIDQEAERHNWEA 320
Cdd:PRK13307 241 LEARMAADATADAVVISGLAPISTIEKAIHEAQKTGIYSILDMLNVEDPVKLLESLKVKPDVVELHRGIDEEGTEHAWGN 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504398499 321 IAEIKRMaassDRKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELKQtEIDQYRVMTDF 396
Cdd:PRK13307 321 IKEIKKA----GGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKLKP-DIDQFRLMTDF 391
|
|
| Fae |
COG1795 |
Formaldehyde-activating enzyme (5,6,7,8-tetrahydromethanopterin hydrolyase) [Energy production ... |
1-166 |
3.14e-104 |
|
Formaldehyde-activating enzyme (5,6,7,8-tetrahydromethanopterin hydrolyase) [Energy production and conversion];
Pssm-ID: 441400 Cd Length: 171 Bit Score: 304.83 E-value: 3.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 1 MFLIGEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFG 80
Cdd:COG1795 5 MMLIGEALVGDGNEVAHIDLIIGPRDGPVGTAFANALANQSAGHTPLLAVLAPNLPVKPATLMVPKVTIKNAKQANQMFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 81 PAQNAVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHP 160
Cdd:COG1795 85 PAQAAVAKAVADAVAEGVIPKDEADDLVIIVSVFIHPEADDDKKIYRYNYEATKLAIKRAMAGEPSIDEVLANKDRAKHP 164
|
....*.
gi 504398499 161 IMGFRV 166
Cdd:COG1795 165 FAGFKV 170
|
|
| one_C_fae |
TIGR03126 |
formaldehyde-activating enzyme; This family consists of formaldehyde-activating enzyme, or the ... |
2-161 |
2.34e-99 |
|
formaldehyde-activating enzyme; This family consists of formaldehyde-activating enzyme, or the corresponding domain of longer, bifunctional proteins. It links formaldehyde to the C1 carrier tetrahydromethanopterin (H4MPT), an analog of tetrahydrofolate, and is common among species with H4MPT. The ribulose monophosphate (RuMP) pathway, which removes the toxic metabolite formaldehyde by assimilation, runs in the opposite direction in some species to produce ribulose 5-phosphate for nucleotide biosynthesis, leaving formaldehyde as an additional metabolite. In these species, formaldehyde activating enzyme may occur as a fusion protein with D-arabino 3-hexulose 6-phosphate formaldehyde lyase from the RuMP pathway.
Pssm-ID: 132170 Cd Length: 160 Bit Score: 292.33 E-value: 2.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 2 FLIGEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFGP 81
Cdd:TIGR03126 1 YRIGEALIGEGNEVAHIDLIIGPKGGPVGTAFANALANLSAGHTPLLAVLRPNLPTKPATLIVPKVTIKNMAQAVQMFGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 82 AQNAVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHPI 161
Cdd:TIGR03126 81 AQAAVAKAVADSVEEGIIPKDEADDLVIIVSVFIHPEAKDDRKIYKYNYEATKLAIKRAMEGEPSVDEVLAKKDSATHPF 160
|
|
| Fae |
pfam08714 |
Formaldehyde-activating enzyme (Fae); Formaldehyde-activating enzyme is an enzyme required for ... |
5-162 |
5.81e-98 |
|
Formaldehyde-activating enzyme (Fae); Formaldehyde-activating enzyme is an enzyme required for energy metabolism and formaldehyde detoxification. It catalyzes the condensation of formaldehyde and tetrahydromethanopterin to methylene tetrahydromethanopterin.
Pssm-ID: 430170 Cd Length: 158 Bit Score: 288.69 E-value: 5.81e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 5 GEALIGDEPELAHVDLLIGDKDGPVGTAFASGLAQLSAGHTPLLSVIRPNLPPKPATLIVPKVTVKNMEQAAAIFGPAQN 84
Cdd:pfam08714 1 GEALVGEGNEVAHIDLIIGPKGGPVGTAFANALTNQSAGHTPLLAVLRPNLMVKPATLMVPKVTIKNMKQAELMFGPAQA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504398499 85 AVAKAVADSVAEGVIPKAEVENLVVIASVFIHPQARDYDAIYRYNYGATKLAVKRAMEGFPDIDTVLYEKDRSTHPIM 162
Cdd:pfam08714 81 AVAKAVADAVEEGIIPKDEADDLVIIVSVFIHPDALDKRKIYRYNYEATKLAIKRAMAGEPSIDEVLAEKDRAKHPFM 158
|
|
| UlaD |
COG0269 |
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism]; |
170-385 |
2.94e-69 |
|
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
Pssm-ID: 440039 Cd Length: 212 Bit Score: 217.34 E-value: 2.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 170 WDPPYLQVALDLVDLTVVRRVLSQlPDSDHLLIEVGTPLVKKFGASVVKEIRNVRPSSFVVLDLKTLDTGNLEVRLAADA 249
Cdd:COG0269 1 MMKPKLQVALDLLDLDEALAIAKE-VAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 250 TADAVVISGLAPQKTLELAIREARKTGIYSVIDMLNVPDPLEVLRSLAVL-PDVVEMHRAIDQEAERHN-WEAIAEIKRM 327
Cdd:COG0269 80 GADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELgVDIVILHRGIDAQAAGGSpLDDLKKIKEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504398499 328 AassdrKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELKQT 385
Cdd:COG0269 160 V-----GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDKA 212
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
173-378 |
3.76e-64 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 203.58 E-value: 3.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 173 PYLQVALDLVDLTVVRRVLSQLPDSdHLLIEVGTPLVKKFGASVVKEIRNVRPSSFVVLDLKTLDTGNLEVRLAADATAD 252
Cdd:cd04726 1 PLLQVALDLLDLEEALELAKKVPDG-VDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 253 AVVISGLAPQKTLELAIREARKTGIYSVIDMLNVPDPLEVLRSLAVLPDVVEMHRAIDQEAERhNWEAIAEIKRMaaSSD 332
Cdd:cd04726 80 IVTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAG-GWWPEDDLKKV--KKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504398499 333 RKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:cd04726 157 LGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
173-378 |
2.03e-32 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 126.67 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 173 PYLQVALDLVDLTVVRRVLSQLPDSDHLLIEVGTPLVKKFGASVVKEIRNVRPSSFVVLDLKTLDTGNLEVRLAADATAD 252
Cdd:PRK07028 4 PILQVALDLLELDRAVEIAKEAVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 253 AVVISGLAPQKTLELAIREARKTGIYSVIDMLNVPDPLEVLRSLAVLP-DVVEMHRAIDQEAErhNWEAIAEIKRMaaSS 331
Cdd:PRK07028 84 IVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGvDYINVHVGIDQQML--GKDPLELLKEV--SE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504398499 332 DRKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:PRK07028 160 EVSIPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKI 206
|
|
| OMPdecase |
smart00934 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ... |
174-378 |
1.35e-29 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 113.80 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 174 YLQVALDLVDLTVVRRVLSQLPDSdHLLIEVGTPLVKKFGASVVKEIRNVRPSsFVVLDLKTLDTGNLEVRLAADATADA 253
Cdd:smart00934 1 RLIVALDVPDLEEALELADALGDS-VDIIKVGTELFLAEGPEGVKELKELFGF-PVFLDLKLHDIPNTVARAARAAAELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 254 VV---ISGLAPQKTLELAIREARKTG-IYSVIDMLNVPDPLEV--------------LRSLAVLPDVVEMHRAIDQeaer 315
Cdd:smart00934 79 ADavtVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLqelgdesleeqvlrLAKLAKEAGLDGVVCSATE---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504398499 316 hnweaiAEIKRMAASSDRKVLVAvagGI----RVDTVASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:smart00934 155 ------PELIRRALGPDFLILTP---GIgdqgRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
|
|
| OMPdecase |
pfam00215 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ... |
173-378 |
4.17e-26 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.
Pssm-ID: 395160 Cd Length: 215 Bit Score: 104.27 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 173 PYLQVALDLVDLTVVRRVLSQLPDSdHLLIEVGTPLVKKFGASVVKEIRNVRpsSFVVLDLKTLDTGNLEVRLAADATAD 252
Cdd:pfam00215 1 PNLCVALDVPTLEEALELADELGPY-VDILKVGTPLFEAFGLKLVAELRKHG--FLIFLDLKFADIGNTVAKQAKYKAKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 253 ---AVVISGLAPQKTLELAIREARKTG-IYSVIDMLNVPDPLEVLRSLAVLPDVVEMHRAIDQEAERHNWEAIAEIKRMA 328
Cdd:pfam00215 78 gadIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLAAGVDGVVASATEALRE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504398499 329 ASSDRKVLV-------AVAGGIRVDTV-ASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:pfam00215 158 ILPDFLILTpgiglqgGDAGGQQRVTTpAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
|
|
| ulaD |
PRK13306 |
3-dehydro-L-gulonate-6-phosphate decarboxylase; |
173-390 |
5.84e-11 |
|
3-dehydro-L-gulonate-6-phosphate decarboxylase;
Pssm-ID: 237344 Cd Length: 216 Bit Score: 61.87 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 173 PYLQVALDLVDLTVVRRVLSQLPDS-DhlLIEVGTPLVKKFGASVVKEIRNVRPSSFVVLDLKTLDTGNLEVRLAADATA 251
Cdd:PRK13306 4 PLLQIALDNQDLESAIEDAKKVAEEvD--IIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 252 DAVVISGLAPQKTLELAIREARKTG------IYSVIDMLNVPDPLEVLRSLAVlpdvveMHRAIDQEAERHNWEAiAEIK 325
Cdd:PRK13306 82 DWVTVICAAHIPTIKAALKVAKEFNgeiqieLYGNWTWEQAQQWRDAGISQVI------YHRSRDAQLAGVAWGE-KDLN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504398499 326 RMAASSDRKVLVAVAGGIRVDTVasALSSGAD--IVVTGRAITGSKDVRDAAEQFlaelkQTEIDQY 390
Cdd:PRK13306 155 KVKKLSDMGFKVSVTGGLVVEDL--KLFKGIPvkTFIAGRAIRGAADPAAAARAF-----KDEIAKY 214
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
321-384 |
8.62e-09 |
|
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439806 Cd Length: 218 Bit Score: 55.47 E-value: 8.62e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504398499 321 IAEIKRMAASSDRKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELKQ 384
Cdd:COG0036 154 IRRLRELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAA 217
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
318-378 |
2.88e-07 |
|
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.
Pssm-ID: 238244 Cd Length: 211 Bit Score: 50.56 E-value: 2.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504398499 318 WEAIAEIKRMAASSDRKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:cd00429 150 LEKIRKLRELIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
|
|
| OMP_decarboxylase_like |
cd04725 |
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ... |
177-378 |
1.14e-06 |
|
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.
Pssm-ID: 240076 Cd Length: 216 Bit Score: 49.10 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 177 VALDLVDLTVVRRVLSQLPDSDhLLIEVGTPLVKKFGASVVKEIRNVrpSSFVVLDLKTLDTGN---LEVRLAADATADA 253
Cdd:cd04725 3 VALDPPDEEFALALIDALGPYV-CAVKVGLELFEAAGPEIVKELREL--GFLVFLDLKLGDIPNtvaAAAEALLGLGADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 254 VVISGLAPQKTLE--LAIREARKTGIYSVIDMLNvPDPLEVLRSLAVLPDVVEMHRAidQEAERHN--------WEAiaE 323
Cdd:cd04725 80 VTVHPYGGSDMLKaaLEAAEEKGKGLFAVTVLSS-PGALDLQEGIPGSLEDLVERLA--KLAREAGvdgvvcgaTEP--E 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504398499 324 IKRMAASSDRKVLV-------AVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQF 378
Cdd:cd04725 155 ALRRALGPDFLILTpgigaqgSGDDQKRGGTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
|
|
| PRK00230 |
PRK00230 |
orotidine-5'-phosphate decarboxylase; |
177-382 |
4.35e-06 |
|
orotidine-5'-phosphate decarboxylase;
Pssm-ID: 234695 Cd Length: 230 Bit Score: 47.44 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 177 VALDLVDLTVVRRVLSQLPDSDhLLIEVGTPLVKKFGASVVKEIRNVRPSSFvvLDLKTLDTGNlevrlaadatadavvi 256
Cdd:PRK00230 7 VALDFPSKEEALAFLDQLDPAV-LFVKVGMELFTAGGPQFVRELKQRGFKVF--LDLKLHDIPN---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 257 sglapqkTLELAIREARKTGIysviDMLNV-------------------PDPL------------EVLRSLAV---LPDV 302
Cdd:PRK00230 68 -------TVAKAVRALAKLGV----DMVNVhasggprmmkaarealepkSRPLliavtvltsmdeEDLAELGInlsLEEQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 303 VEmHRA-------ID------QEAerhnweaiAEIKRmAASSDRKVlvaVAGGIR-----------VDTVASALSSGADI 358
Cdd:PRK00230 137 VL-RLAklaqeagLDgvvcsaQEA--------AAIRE-ATGPDFLL---VTPGIRpagsdagdqkrVMTPAQAIAAGSDY 203
|
250 260
....*....|....*....|....
gi 504398499 359 VVTGRAITGSKDVRDAAEQFLAEL 382
Cdd:PRK00230 204 IVVGRPITQAADPAAAYEAILAEI 227
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
324-385 |
4.36e-06 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 47.10 E-value: 4.36e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504398499 324 IKRMAASSDRKVLVAVaGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELKQT 385
Cdd:PRK00043 151 LREIRAAVGDIPIVAI-GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
|
|
| PRK13813 |
PRK13813 |
orotidine 5'-phosphate decarboxylase; Provisional |
173-383 |
1.86e-05 |
|
orotidine 5'-phosphate decarboxylase; Provisional
Pssm-ID: 237520 Cd Length: 215 Bit Score: 45.36 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 173 PYLQVALDLVDLTVVRRVLSQLPDSdHLLIEVGTPLVKKFGASVVKEIRNVRPssfVVLDLKTLDTGNlEVRLAADATAD 252
Cdd:PRK13813 4 SRIILALDVTDRERALKIAEELDDY-VDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADIPN-TNRLICEAVFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 253 A----VVISGLAPQKTLELAIREARKTG--IYSVIDMlNVPDPLEVLRSLAVlpDVVEMHRAID--------QEAERhnw 318
Cdd:PRK13813 79 AgawgIIVHGFTGRDSLKAVVEAAAESGgkVFVVVEM-SHPGALEFIQPHAD--KLAKLAQEAGafgvvapaTRPER--- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504398499 319 eaIAEIKRMAAssdrKVLVAVAGGIRVD--TVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELK 383
Cdd:PRK13813 153 --VRYIRSRLG----DELKIISPGIGAQggKAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIR 213
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
321-383 |
1.16e-04 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 42.86 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504398499 321 IAEIKRMAASSDRKVLVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELK 383
Cdd:PRK05581 157 IRELRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELA 219
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
321-385 |
1.20e-04 |
|
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: 42.86 E-value: 1.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504398499 321 IAEIKRMAASSDRKVlvaVA-GGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELKQT 385
Cdd:COG0352 144 LEGLAWWAELVEIPV---VAiGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| PyrF |
COG0284 |
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ... |
344-384 |
3.60e-04 |
|
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440053 Cd Length: 228 Bit Score: 41.63 E-value: 3.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 504398499 344 RVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLAELKQ 384
Cdd:COG0284 188 RVGTPAEAIAAGADYLVVGRPITYAGDPRAAAEAIREEIAA 228
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
320-383 |
4.20e-04 |
|
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: 42.04 E-value: 4.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504398499 320 AIAEIKRMAASSDRKVLVAVAGGIRVDT-VASALSSGADIVVTGR------AITGSKDVRDAAEQFLAELK 383
Cdd:cd04737 262 SFDSLPEIAEAVNHRVPIIFDSGVRRGEhVFKALASGADAVAVGRpvlyglALGGAQGVASVLEHLNKELK 332
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
319-365 |
2.33e-03 |
|
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.
Pssm-ID: 395672 Cd Length: 198 Bit Score: 38.85 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 504398499 319 EAIAEIKRMAASSDRKVLVAVAGGIRVDTVASALSSGADIVVTGRAI 365
Cdd:pfam00834 151 EKIRKVRKMIDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
321-374 |
3.55e-03 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 38.44 E-value: 3.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 504398499 321 IAEIKRMAASSDrkvlVAVAGGIRVDTVASALSSGADIVVTGRAITGSKDVRDA 374
Cdd:PLN02334 165 VRALRKKYPELD----IEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEV 214
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
321-380 |
3.57e-03 |
|
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: 38.27 E-value: 3.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504398499 321 IAEIKRMAASSDRKVlVAVaGGIRVDTVASALSSGADIVVTGRAITGSKDVRDAAEQFLA 380
Cdd:cd00564 139 LELLREIAELVEIPV-VAI-GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| |
