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Conserved domains on  [gi|581787504|gb|EVR90720|]
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UDP-N-acetylenolpyruvoylglucosamine reductase [Staphylococcus aureus M1470]

Protein Classification

UDP-N-acetylmuramate dehydrogenase( domain architecture ID 11486943)

UDP-N-acetylmuramate dehydrogenase is responsible for the synthesis of UDP-N-acetylmuramic acid in bacterial cell wall biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-307 0e+00

UDP-N-acetylmuramate dehydrogenase;


:

Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 616.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  81 GIVISLLSLDHIDVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581787504 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
 
Name Accession Description Interval E-value
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-307 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 616.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  81 GIVISLLSLDHIDVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581787504 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 23-300 5.35e-146

UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440574 [Multi-domain]  Cd Length: 279  Bit Score: 411.33  E-value: 5.35e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  23 EPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIDVSDDAII-A 101
Cdd:COG0812    1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 102 GSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSIIQ 181
Cdd:COG0812   81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 182 KEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAG 261
Cdd:COG0812  161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 581787504 262 FMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRII 300
Cdd:COG0812  241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 25-301 7.58e-81

UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 272945 [Multi-domain]  Cd Length: 284  Bit Score: 246.21  E-value: 7.58e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   25 LKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSL-DHIDVSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGiDIEDDEGEYVHVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSIIQKE 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  184 HL-VVLEAAFTLAPGKMTE-----IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVST 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGFGTRldpetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 581787504  258 KHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 202-300 3.81e-54

UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 460730 [Multi-domain]  Cd Length: 99  Bit Score: 171.38  E-value: 3.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  202 IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80

                          90
                  ....*....|....*....
gi 581787504  282 QKTVKEKFGIELNREVRII 300
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
 
Name Accession Description Interval E-value
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-307 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 616.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  81 GIVISLLSLDHIDVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581787504 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
14-302 4.01e-164

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 458.04  E-value: 4.01e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  14 IPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISL-LSLDHI 92
Cdd:PRK13905   8 ALRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLgKGLNEI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  93 DVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELE 172
Cdd:PRK13905  88 EVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKTLSNEELG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 173 LDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGG 252
Cdd:PRK13905 168 FGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLKGYRIGG 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 581787504 253 VEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
Cdd:PRK13905 248 AQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGE 297
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 23-300 5.35e-146

UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440574 [Multi-domain]  Cd Length: 279  Bit Score: 411.33  E-value: 5.35e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  23 EPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIDVSDDAII-A 101
Cdd:COG0812    1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 102 GSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSIIQ 181
Cdd:COG0812   81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 182 KEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAG 261
Cdd:COG0812  161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 581787504 262 FMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRII 300
Cdd:COG0812  241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
1-302 3.78e-145

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 410.55  E-value: 3.78e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK12436   1 MNMQEVYEYLSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  81 GIVISLLSLDHIDVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK12436  81 GITVSLIHITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMTGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK12436 161 GELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEGVYEEIKAKMDDLTFKRESKQPLEYPSCGSVFKRPPNNFAGKLI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581787504 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
Cdd:PRK12436 241 QESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIGE 302
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 25-301 7.58e-81

UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 272945 [Multi-domain]  Cd Length: 284  Bit Score: 246.21  E-value: 7.58e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   25 LKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSL-DHIDVSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGiDIEDDEGEYVHVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSIIQKE 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  184 HL-VVLEAAFTLAPGKMTE-----IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVST 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGFGTRldpetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 581787504  258 KHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
22-301 1.30e-66

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 210.47  E-value: 1.30e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  22 DEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLD---HIDVSDDA 98
Cdd:PRK14649   6 NEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYRGQRwelHEHGDTAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  99 IIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNS 178
Cdd:PRK14649  86 VWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLLLNGSECVEWSVHDFAYGYRTS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 179 IIQK--------EHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEyPSCGSVFQRPPGHFAGKLIQDSNLQGHRI 250
Cdd:PRK14649 166 VLKQlradgitwRPPLVLAARFRLHRDDPTALAARMEAIAAERKQKTPAG-SSCGSVFKNPPGDSAGRLIEAAGLKGTRI 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 581787504 251 GGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:PRK14649 245 GDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
18-302 7.88e-64

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 203.57  E-value: 7.88e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  18 KIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIDVSDD 97
Cdd:PRK14652  17 EVLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGESTDG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  98 A-IIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIkLTTKELELDYR 176
Cdd:PRK14652  97 GrLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVTAVELATADGAGF-VPAAALGYAYR 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 177 NSIIQKEHlVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVS 256
Cdd:PRK14652 176 TCRLPPGA-VITRVEVRLRPGDVAASEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGHRVGGAIWS 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 581787504 257 TKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
Cdd:PRK14652 255 PVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLGE 300
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
21-299 5.58e-62

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 198.52  E-value: 5.58e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  21 VDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYaYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIDVSDDAII 100
Cdd:PRK14653  18 INEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINL-LKEGIEVKILGNGTNVLPKDEPMDFVVVSTERLDDIFVDNDKII 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 101 AGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALcVNEQGSLIKLTTKELELDYRNSII 180
Cdd:PRK14653  97 CESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVEVV-AYDGKKIIRLGKNEIKFSYRNSIF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 181 QKE-HLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRP-PGHFAGKLIQDSNLQGHRIGGVEVSTK 258
Cdd:PRK14653 176 KEEkDLIILRVTFKLKKGNKNEIYNLMLETMKKRVEKQPLEFPSAGSVFKRPrKDFYVGSAIEKLGLKGFSIGGAQISEK 255

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 581787504 259 HAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRI 299
Cdd:PRK14653 256 HAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEIEI 296
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 202-300 3.81e-54

UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 460730 [Multi-domain]  Cd Length: 99  Bit Score: 171.38  E-value: 3.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  202 IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80

                          90
                  ....*....|....*....
gi 581787504  282 QKTVKEKFGIELNREVRII 300
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
PRK14650 PRK14650
UDP-N-acetylmuramate dehydrogenase;
25-301 5.13e-45

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173113 [Multi-domain]  Cd Length: 302  Bit Score: 155.00  E-value: 5.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  25 LKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGG-IRGIVISLLSLDHIDVSDDAIIAGS 103
Cdd:PRK14650  21 LANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEeIDFPIIYTGHLNKIEIHDNQIVAEC 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSIIQKE 183
Cdd:PRK14650 101 GTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKITFIDEKGKTICKKFKKEEFKYKISPFQNK 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 184 HLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHF--AGKLIQDSNLQGHRIGGVEVSTKHAG 261
Cdd:PRK14650 181 NTFILKATLNLKKGNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNNKAFLkpTGQIIEECKLKGLSIGGATVSHYHGN 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 581787504 262 FMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:PRK14650 261 FIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
24-306 5.27e-41

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 143.42  E-value: 5.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  24 PLKRYTYTKTGGNADFYITPTKNEEVQAVvkyayqnEIPVTYLGNGSNIIIREGGIRGIVISLlSLDHIDVSDDAIIaGS 103
Cdd:PRK14651   8 PLARYTTLGVGGPAELWTVETHEQLAEAT-------EAPYRVLGGGSNLLVSDAGVPERVIRL-GGEFAEWDLDGWV-GG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGsLIKLTTKELELDYRNSIIQKE 183
Cdd:PRK14651  79 GVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVHDGG-FHQYSPDELGFGYRHSGLPPG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 184 HlVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGsvFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFM 263
Cdd:PRK14651 158 H-VVTRVRLKLRPSTPEAVLAKMALVDAARKGQPKKKSAGCA--FKNPPGDSAGRLIDEAGLKGTRVGDAMISPEHGNFI 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 581787504 264 VNVDNGTATDyenlIHYVQKTVKEKFGIELNREVRIIGEHPKE 306
Cdd:PRK14651 235 VNLGGATAAD----VHALLRRVRARVGLPLELEWELWPEQLPE 273
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
114-300 3.16e-40

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 140.83  E-value: 3.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 114 ARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDyALCVNeQGSLIKlttKELELDYRNSIIQKehlVVLEAAFT 193
Cdd:PRK13904  84 AKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLE-SICTN-GGWIEK---EDIGFGYRSSGING---VILEARFK 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 194 LAPGKMTEIQakmDDLTERRESkQPLEyPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATD 273
Cdd:PRK13904 156 KTHGFDEELL---EAFKSMRKN-QPKG-PSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGAGFSEEHANFLVNLGGATFED 230

                        170       180
                 ....*....|....*....|....*..
gi 581787504 274 YENLIHYVQKTVKEKFGIELNREVRII 300
Cdd:PRK13904 231 ALDLIELAKKRVLEEFGINLEEEVIIL 257
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
24-302 7.16e-35

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 129.46  E-value: 7.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  24 PLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLD--HIDVSDDAII- 100
Cdd:PRK14648  17 PLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRRFRslHTQTQRDGSVl 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 101 --AGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYAL----------------------- 155
Cdd:PRK14648  97 vhAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARtlvlhpvrsrakelpevrknaqd 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 156 ----CVNEQG------SLIKLTTKELELDYRNSIIQKEHLVVLEAA--------FTLAPGKMTEIQAKMDDLTERRESKQ 217
Cdd:PRK14648 177 krgeCLGLDGgpftcsSFQTVFARAGDWGYKRSPFQSPHGVELHAGrrlilslcVRLTPGNPAQIRKHMQEKIADRISKG 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 218 PLEYPSCGSVFQRPP--GHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNR 295
Cdd:PRK14648 257 QFRFPSAGSAFKNNPafGKPSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQRVFETHGVWLER 336


                 ....*..
gi 581787504 296 EVRIIGE 302
Cdd:PRK14648 337 EIIFSGE 343
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
36-300 3.40e-31

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 119.09  E-value: 3.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  36 NADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGgIRGIVI--SLLSLDHIDVSDDAII--AGSGAAIID-V 110
Cdd:PRK00046  20 RARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTED-FDGTVLlnRIKGIEVLSEDDDAWYlhVGAGENWHDlV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 111 SR-VARDYAltGLE-FACgIPGSIGGAVYMNAGAYGGEVKDCIDYALCVN-EQGSLIKLTTKELELDYRNSI-------- 179
Cdd:PRK00046  99 LWtLQQGMP--GLEnLAL-IPGTVGAAPIQNIGAYGVELKDVCDYVEALDlATGEFVRLSAAECRFGYRDSIfkheypdr 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 180 ---------IQKEHLVVLEAA--FTLAPGKMTeIQAKMDDLTERRESK--QPLEYPSCGSVFQRP--------------P 232
Cdd:PRK00046 176 yaitavgfrLPKQWQPVLDYGdlARLDPDTVT-AQDVFDAVCAIRRSKlpDPKVLGNAGSFFKNPvvsaeqfeallaqyP 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 233 G--HF----------AGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRII 300
Cdd:PRK00046 255 DipHYpqadgsvklaAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLALARHIQQDVREKFGVELEPEPRFI 334
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 37-167 2.12e-28

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 106.52  E-value: 2.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   37 ADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHI---DVSDDAIIAGSGAAIIDVSRV 113
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRLNGIleiDPEDGTATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 581787504  114 ARDYALT-GLEFACGIPGSIGGAVYMNAGAYGGE----VKDCIDYALCVNEQGSLIKLT 167
Cdd:pfam01565  81 LAAKGLLlGLDPGSGIPGTVGGAIATNAGGYGSEkyglTRDNVLGLEVVLADGEVVRLG 139
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
22-301 8.22e-26

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 105.04  E-value: 8.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  22 DEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLD-HIDVSDDAII 100
Cdd:PRK13903  18 DVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVVRVATRGvTVDCGGGLVR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 101 AGSGAAIIDVsrVARDYA--LTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCI------DYALcvneqGSLIKLTTKELE 172
Cdd:PRK13903  98 AEAGAVWDDV--VARTVEagLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTItrvrllDRRT-----GEVRWVPAADLG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 173 LDYRNSII-QKEHLVVLEAAFTLAPGKMT------EIQAKMD-------DLTERRE-------SKQPLEYP------SCG 225
Cdd:PRK13903 171 FGYRTSVLkHSDRAVVLEVEFQLDPSGLSaplrygELARALGvepgervPPAAVREavlalraGKGMVLDPadhdtwSAG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504 226 SVFQRP----------------------------PGHF---AGKLIQDSNL-QGHRIGG--VEVSTKHAGFMVNVDNGTA 271
Cdd:PRK13903 251 SFFTNPvvspavaerlaarvaerlgdpvprypagDGGVklsAAWLIERAGFgKGYPGGGapARLSTKHTLALTNRGGATT 330

                        330       340       350
                 ....*....|....*....|....*....|
gi 581787504 272 TDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:PRK13903 331 ADLVALAREVRDGVRDAFGVTLVPEPVLVG 360
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
1-144 5.42e-11

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 62.99  E-value: 5.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTG---GNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIiirEG 77
Cdd:COG0277    1 MLTAALLAALRAILAGRVLTDPADRAAYARDGNSlyrGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGL---AG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581787504  78 GI----RGIVISLLSLDHI---DVSDDAIIAGSGAAIIDVSRVARDYaltGLEFACGiPGS-----IGGAVYMNAG---- 141
Cdd:COG0277   78 GAvpldGGVVLDLSRMNRIlevDPEDRTATVEAGVTLADLNAALAPH---GLFFPPD-PSSqgtatIGGNIATNAGgprs 153


                 ....
gi 581787504 142 -AYG 144
Cdd:COG0277  154 lKYG 157
 
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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