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Conserved domains on  [gi|446531089|ref|WP_000608435|]
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MULTISPECIES: UDP-N-acetylmuramate dehydrogenase [Staphylococcus]

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: 614.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 161 GSIIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531089 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: 614.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 161 GSIIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531089 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
23-300 4.92e-147

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: 414.03  E-value: 4.92e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  23 EPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDDAII-A 101
Cdd:COG0812    1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 102 GSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSIIKLTTKELELDYRNSIIQ 181
Cdd:COG0812   81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 182 KEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAG 261
Cdd:COG0812  161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 446531089 262 FMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRII 300
Cdd:COG0812  241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
25-301 9.63e-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: 9.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   25 LKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSL-DHIEVSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGiDIEDDEGEYVHVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSIIKLTTKELELDYRNSIIQKE 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  184 HL-VVLEAAFTLAPGKMTE-----IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVST 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGFGTRldpetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 446531089  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 5.38e-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: 170.99  E-value: 5.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  202 IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
                          90
                  ....*....|....*....
gi 446531089  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: 614.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 161 GSIIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531089 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
14-302 2.06e-164

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 458.81  E-value: 2.06e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  14 IPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISL-LSLDHI 92
Cdd:PRK13905   8 ALRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLgKGLNEI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  93 EVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSIIKLTTKELE 172
Cdd:PRK13905  88 EVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKTLSNEELG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 173 LDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGG 252
Cdd:PRK13905 168 FGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLKGYRIGG 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446531089 253 VEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
Cdd:PRK13905 248 AQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGE 297
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
23-300 4.92e-147

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: 414.03  E-value: 4.92e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  23 EPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDDAII-A 101
Cdd:COG0812    1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 102 GSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSIIKLTTKELELDYRNSIIQ 181
Cdd:COG0812   81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 182 KEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAG 261
Cdd:COG0812  161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 446531089 262 FMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRII 300
Cdd:COG0812  241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
1-302 1.12e-144

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 409.40  E-value: 1.12e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK12436   1 MNMQEVYEYLSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK12436  81 GITVSLIHITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMTGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 161 GSIIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK12436 161 GELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEGVYEEIKAKMDDLTFKRESKQPLEYPSCGSVFKRPPNNFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531089 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
Cdd:PRK12436 241 QESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIGE 302
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
25-301 9.63e-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: 9.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   25 LKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSL-DHIEVSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGiDIEDDEGEYVHVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSIIKLTTKELELDYRNSIIQKE 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  184 HL-VVLEAAFTLAPGKMTE-----IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVST 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGFGTRldpetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 446531089  258 KHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
22-301 4.37e-67

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 211.62  E-value: 4.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  22 DEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLD---HIEVSDDA 98
Cdd:PRK14649   6 NEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYRGQRwelHEHGDTAE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  99 IIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSIIKLTTKELELDYRNS 178
Cdd:PRK14649  86 VWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLLLNGSECVEWSVHDFAYGYRTS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 179 IIQK--------EHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEyPSCGSVFQRPPGHFAGKLIQDSNLQGHRI 250
Cdd:PRK14649 166 VLKQlradgitwRPPLVLAARFRLHRDDPTALAARMEAIAAERKQKTPAG-SSCGSVFKNPPGDSAGRLIEAAGLKGTRI 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446531089 251 GGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:PRK14649 245 GDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
18-302 1.13e-64

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 205.49  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  18 KIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDD 97
Cdd:PRK14652  17 EVLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGESTDG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  98 A-IIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDyALCVNEQGSIIKLTTKELELDYR 176
Cdd:PRK14652  97 GrLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVT-AVELATADGAGFVPAAALGYAYR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 177 NSIIQKEHlVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVS 256
Cdd:PRK14652 176 TCRLPPGA-VITRVEVRLRPGDVAASEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGHRVGGAIWS 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446531089 257 TKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
Cdd:PRK14652 255 PVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLGE 300
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
21-299 6.59e-63

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 200.83  E-value: 6.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  21 VDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYaYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDDAII 100
Cdd:PRK14653  18 INEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINL-LKEGIEVKILGNGTNVLPKDEPMDFVVVSTERLDDIFVDNDKII 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 101 AGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALcVNEQGSIIKLTTKELELDYRNSII 180
Cdd:PRK14653  97 CESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVEVV-AYDGKKIIRLGKNEIKFSYRNSIF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 181 QKE-HLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRP-PGHFAGKLIQDSNLQGHRIGGVEVSTK 258
Cdd:PRK14653 176 KEEkDLIILRVTFKLKKGNKNEIYNLMLETMKKRVEKQPLEFPSAGSVFKRPrKDFYVGSAIEKLGLKGFSIGGAQISEK 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446531089 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 5.38e-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: 170.99  E-value: 5.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  202 IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
                          90
                  ....*....|....*....
gi 446531089  282 QKTVKEKFGIELNREVRII 300
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
PRK14650 PRK14650
UDP-N-acetylmuramate dehydrogenase;
25-301 1.81e-45

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173113 [Multi-domain]  Cd Length: 302  Bit Score: 156.16  E-value: 1.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  25 LKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGG-IRGIVISLLSLDHIEVSDDAIIAGS 103
Cdd:PRK14650  21 LANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEeIDFPIIYTGHLNKIEIHDNQIVAEC 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSIIKLTTKELELDYRNSIIQKE 183
Cdd:PRK14650 101 GTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKITFIDEKGKTICKKFKKEEFKYKISPFQNK 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 184 HLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHF--AGKLIQDSNLQGHRIGGVEVSTKHAG 261
Cdd:PRK14650 181 NTFILKATLNLKKGNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNNKAFLkpTGQIIEECKLKGLSIGGATVSHYHGN 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446531089 262 FMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:PRK14650 261 FIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
24-306 5.92e-41

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 143.42  E-value: 5.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  24 PLKRYTYTKTGGNADFYITPTKNEEVQAVvkyayqnEIPVTYLGNGSNIIIREGGIRGIVISLlSLDHIEVSDDAIIaGS 103
Cdd:PRK14651   8 PLARYTTLGVGGPAELWTVETHEQLAEAT-------EAPYRVLGGGSNLLVSDAGVPERVIRL-GGEFAEWDLDGWV-GG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 104 GAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGsIIKLTTKELELDYRNSIIQKE 183
Cdd:PRK14651  79 GVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVHDGG-FHQYSPDELGFGYRHSGLPPG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 184 HlVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGsvFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFM 263
Cdd:PRK14651 158 H-VVTRVRLKLRPSTPEAVLAKMALVDAARKGQPKKKSAGCA--FKNPPGDSAGRLIDEAGLKGTRVGDAMISPEHGNFI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446531089 264 VNVDNGTATDyenlIHYVQKTVKEKFGIELNREVRIIGEHPKE 306
Cdd:PRK14651 235 VNLGGATAAD----VHALLRRVRARVGLPLELEWELWPEQLPE 273
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
88-300 9.92e-41

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 142.37  E-value: 9.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  88 SLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDyALCVNeQGSIIKlt 167
Cdd:PRK13904  58 NFDYIKIDGECLEIGGATKSGKIFNYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLE-SICTN-GGWIEK-- 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 168 tKELELDYRNSIIQKehlVVLEAAFTLAPGKMTEIQakmDDLTERRESkQPLEyPSCGSVFQRPPGHFAGKLIQDSNLQG 247
Cdd:PRK13904 134 -EDIGFGYRSSGING---VILEARFKKTHGFDEELL---EAFKSMRKN-QPKG-PSFGSCFKNPKGDYAGRLIEAVGLKG 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446531089 248 HRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRII 300
Cdd:PRK13904 205 YCKGGAGFSEEHANFLVNLGGATFEDALDLIELAKKRVLEEFGINLEEEVIIL 257
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
24-302 4.04e-35

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 130.23  E-value: 4.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  24 PLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLD--HIEVSDDAII- 100
Cdd:PRK14648  17 PLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRRFRslHTQTQRDGSVl 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 101 --AGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYAL----------------------- 155
Cdd:PRK14648  97 vhAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARtlvlhpvrsrakelpevrknaqd 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 156 ----CVNEQG------SIIKLTTKELELDYRNSIIQKEHLVVLEAA--------FTLAPGKMTEIQAKMDDLTERRESKQ 217
Cdd:PRK14648 177 krgeCLGLDGgpftcsSFQTVFARAGDWGYKRSPFQSPHGVELHAGrrlilslcVRLTPGNPAQIRKHMQEKIADRISKG 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 218 PLEYPSCGSVFQRPP--GHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNR 295
Cdd:PRK14648 257 QFRFPSAGSAFKNNPafGKPSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQRVFETHGVWLER 336

                 ....*..
gi 446531089 296 EVRIIGE 302
Cdd:PRK14648 337 EIIFSGE 343
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
36-300 1.47e-31

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 120.25  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  36 NADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGgIRGIVI--SLLSLDHIEVSDDAII--AGSGAAIID-V 110
Cdd:PRK00046  20 RARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTED-FDGTVLlnRIKGIEVLSEDDDAWYlhVGAGENWHDlV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 111 SR-VARDYAltGLE-FACgIPGSIGGAVYMNAGAYGGEVKDCIDYALCVN-EQGSIIKLTTKELELDYRNSI-------- 179
Cdd:PRK00046  99 LWtLQQGMP--GLEnLAL-IPGTVGAAPIQNIGAYGVELKDVCDYVEALDlATGEFVRLSAAECRFGYRDSIfkheypdr 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 180 ---------IQKEHLVVLEAA--FTLAPGKMTeIQAKMDDLTERRESK--QPLEYPSCGSVFQRP--------------P 232
Cdd:PRK00046 176 yaitavgfrLPKQWQPVLDYGdlARLDPDTVT-AQDVFDAVCAIRRSKlpDPKVLGNAGSFFKNPvvsaeqfeallaqyP 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 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 1.83e-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: 1.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   37 ADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDDA---IIAGSGAAIIDVSRV 113
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRLNGILEIDPEdgtATVEAGVTLGDLVRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446531089  114 ARDYALT-GLEFACGIPGSIGGAVYMNAGAYGGE----VKDCIDYALCVNEQGSIIKLT 167
Cdd:pfam01565  81 LAAKGLLlGLDPGSGIPGTVGGAIATNAGGYGSEkyglTRDNVLGLEVVLADGEVVRLG 139
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
22-301 9.65e-26

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 105.04  E-value: 9.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  22 DEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLD-HIEVSDDAII 100
Cdd:PRK13903  18 DVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVVRVATRGvTVDCGGGLVR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 101 AGSGAAIIDVsrVARDYA--LTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCI------DYALcvneqGSIIKLTTKELE 172
Cdd:PRK13903  98 AEAGAVWDDV--VARTVEagLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTItrvrllDRRT-----GEVRWVPAADLG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 173 LDYRNSII-QKEHLVVLEAAFTLAPGKMT------EIQAKMD-------DLTERRE-------SKQPLEYP------SCG 225
Cdd:PRK13903 171 FGYRTSVLkHSDRAVVLEVEFQLDPSGLSaplrygELARALGvepgervPPAAVREavlalraGKGMVLDPadhdtwSAG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089 226 SVFQRP----------------------------PGHF---AGKLIQDSNL-QGHRIGG--VEVSTKHAGFMVNVDNGTA 271
Cdd:PRK13903 251 SFFTNPvvspavaerlaarvaerlgdpvprypagDGGVklsAAWLIERAGFgKGYPGGGapARLSTKHTLALTNRGGATT 330
                        330       340       350
                 ....*....|....*....|....*....|
gi 446531089 272 TDYENLIHYVQKTVKEKFGIELNREVRIIG 301
Cdd:PRK13903 331 ADLVALAREVRDGVRDAFGVTLVPEPVLVG 360
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
1-144 1.03e-10

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 62.22  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTG---GNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIiirEG 77
Cdd:COG0277    1 MLTAALLAALRAILAGRVLTDPADRAAYARDGNSlyrGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGL---AG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531089  78 GI----RGIVISLLSLDHI-EVSDDA--IIAGSGAAIIDVSRVARDYaltGLEFACGiPGS-----IGGAVYMNAG---- 141
Cdd:COG0277   78 GAvpldGGVVLDLSRMNRIlEVDPEDrtATVEAGVTLADLNAALAPH---GLFFPPD-PSSqgtatIGGNIATNAGgprs 153

                 ....
gi 446531089 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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