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Conserved domains on  [gi|495382281|ref|WP_008106991|]
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MULTISPECIES: UDP-N-acetylmuramate dehydrogenase [Pantoea]

Protein Classification

UDP-N-acetylmuramate dehydrogenase( domain architecture ID 11477821)

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 PRK00046
UDP-N-acetylmuramate dehydrogenase;
1-332 0e+00

UDP-N-acetylmuramate dehydrogenase;


:

Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 574.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   1 MSSPNTSLEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITI-EEHD 79
Cdd:PRK00046   2 QLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTEDFDGTVLLNRIKGIEVlSEDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  80 EAWHLHVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALHLPTQKIIRLYREECQF 159
Cdd:PRK00046  82 DAWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDYVEALDLATGEFVRLSAAECRF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 160 GYRDSVFKHAMKNDYVIVAVGLRMAKQWKPVLTYGDLTKLNPATVCAWDIFNAICHMRQSKLPDPKITGNVGSFFKNPLI 239
Cdd:PRK00046 162 GYRDSIFKHEYPDRYAITAVGFRLPKQWQPVLDYGDLARLDPDTVTAQDVFDAVCAIRRSKLPDPKVLGNAGSFFKNPVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 240 TAEHATALIKQWPAIPHYPQASGEMKLAAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQ 319
Cdd:PRK00046 242 SAEQFEALLAQYPDIPHYPQADGSVKLAAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLALARHIQQDVRE 321
                        330
                 ....*....|...
gi 495382281 320 KFDVWLEPEVRFI 332
Cdd:PRK00046 322 KFGVELEPEPRFI 334
 
Name Accession Description Interval E-value
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
1-332 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 574.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   1 MSSPNTSLEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITI-EEHD 79
Cdd:PRK00046   2 QLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTEDFDGTVLLNRIKGIEVlSEDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  80 EAWHLHVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALHLPTQKIIRLYREECQF 159
Cdd:PRK00046  82 DAWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDYVEALDLATGEFVRLSAAECRF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 160 GYRDSVFKHAMKNDYVIVAVGLRMAKQWKPVLTYGDLTKLNPATVCAWDIFNAICHMRQSKLPDPKITGNVGSFFKNPLI 239
Cdd:PRK00046 162 GYRDSIFKHEYPDRYAITAVGFRLPKQWQPVLDYGDLARLDPDTVTAQDVFDAVCAIRRSKLPDPKVLGNAGSFFKNPVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 240 TAEHATALIKQWPAIPHYPQASGEMKLAAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQ 319
Cdd:PRK00046 242 SAEQFEALLAQYPDIPHYPQADGSVKLAAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLALARHIQQDVRE 321
                        330
                 ....*....|...
gi 495382281 320 KFDVWLEPEVRFI 332
Cdd:PRK00046 322 KFGVELEPEPRFI 334
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
7-332 2.21e-123

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: 355.86  E-value: 2.21e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   7 SLEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLED-FSGSVVVNA-IKGITIEEHdeaWHL 84
Cdd:COG0812    2 PLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDgFDGLVIRLGrLKGIEVDDG---VLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  85 HVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALHlPTQKIIRLYREECQFGYRDS 164
Cdd:COG0812   79 TAGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLD-RTGEVRTLSAEECGFGYRDS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 165 VFKHamkNDYVIVAVGLRmakqwkpvltygdLTKLNPATVcaWDIFNAICHMRQSKlpDPKITGNVGSFFKNPlitaeha 244
Cdd:COG0812  158 IFKR---ERYIILSVTFR-------------LKKGDPAEI--AAVMDAVLAIRRSK--QPLELPSAGSFFKNP------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 245 talikqwpaiPHYPqasgemklaAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVW 324
Cdd:COG0812  211 ----------PGDS---------AGWLIEQAGLKGYRIGGAQVSEKHANFLVNRGGATAADVLALIEEVQARVKEKFGVE 271

                 ....*...
gi 495382281 325 LEPEVRFI 332
Cdd:COG0812  272 LEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
8-333 1.04e-116

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: 339.04  E-value: 1.04e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281    8 LEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITIEEhDEAWHLHVG 87
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIED-DEGEYVHVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   88 AGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALhLPTQKIIRLYREECQFGYRDSVFK 167
Cdd:TIGR00179  80 GGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATIL-LATGKTEWLTNEQLGFGYRTSIFQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  168 HAMkndyvivaVGLRMAKQWKPVLTYGdlTKLNPATVCAWDIFNAICHMRQSKLPDPkitgNVGSFFKNPLitaehatal 247
Cdd:TIGR00179 159 HKY--------VGLVLKAEFQLTLGFG--TRLDPETITAQQVFNKVCRMRTSHYPDP----NAGSFFKNPS--------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  248 ikqwpaiPHYpqasgemklaAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEP 327
Cdd:TIGR00179 216 -------PNH----------AGRLIEECGLKGYQIGGAAVSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEP 278

                  ....*.
gi 495382281  328 EVRFIG 333
Cdd:TIGR00179 279 EVKIIG 284
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
209-332 2.00e-42

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: 142.49  E-value: 2.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  209 IFNAICHMRQSKL-PDPKITGNVGSFFKNPlitaehatalikqwpaIPHYpqasgemklaAGWLIDQCGLKGFRVGGAAV 287
Cdd:pfam02873   1 IRAAMLELRRRRLaKQPLDPPSAGSFFKNP----------------VGHS----------AGWLIEQAGLKGYRIGGAQV 54
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 495382281  288 HRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFI 332
Cdd:pfam02873  55 SEKHANFLVNTGGATAADVLALIEEVRERVKEKFGVELEPEVRII 99
 
Name Accession Description Interval E-value
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
1-332 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 574.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   1 MSSPNTSLEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITI-EEHD 79
Cdd:PRK00046   2 QLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTEDFDGTVLLNRIKGIEVlSEDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  80 EAWHLHVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALHLPTQKIIRLYREECQF 159
Cdd:PRK00046  82 DAWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDYVEALDLATGEFVRLSAAECRF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 160 GYRDSVFKHAMKNDYVIVAVGLRMAKQWKPVLTYGDLTKLNPATVCAWDIFNAICHMRQSKLPDPKITGNVGSFFKNPLI 239
Cdd:PRK00046 162 GYRDSIFKHEYPDRYAITAVGFRLPKQWQPVLDYGDLARLDPDTVTAQDVFDAVCAIRRSKLPDPKVLGNAGSFFKNPVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 240 TAEHATALIKQWPAIPHYPQASGEMKLAAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQ 319
Cdd:PRK00046 242 SAEQFEALLAQYPDIPHYPQADGSVKLAAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLALARHIQQDVRE 321
                        330
                 ....*....|...
gi 495382281 320 KFDVWLEPEVRFI 332
Cdd:PRK00046 322 KFGVELEPEPRFI 334
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
7-332 2.21e-123

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: 355.86  E-value: 2.21e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   7 SLEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLED-FSGSVVVNA-IKGITIEEHdeaWHL 84
Cdd:COG0812    2 PLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDgFDGLVIRLGrLKGIEVDDG---VLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  85 HVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALHlPTQKIIRLYREECQFGYRDS 164
Cdd:COG0812   79 TAGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLD-RTGEVRTLSAEECGFGYRDS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 165 VFKHamkNDYVIVAVGLRmakqwkpvltygdLTKLNPATVcaWDIFNAICHMRQSKlpDPKITGNVGSFFKNPlitaeha 244
Cdd:COG0812  158 IFKR---ERYIILSVTFR-------------LKKGDPAEI--AAVMDAVLAIRRSK--QPLELPSAGSFFKNP------- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 245 talikqwpaiPHYPqasgemklaAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVW 324
Cdd:COG0812  211 ----------PGDS---------AGWLIEQAGLKGYRIGGAQVSEKHANFLVNRGGATAADVLALIEEVQARVKEKFGVE 271

                 ....*...
gi 495382281 325 LEPEVRFI 332
Cdd:COG0812  272 LEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
8-333 1.04e-116

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: 339.04  E-value: 1.04e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281    8 LEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITIEEhDEAWHLHVG 87
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIED-DEGEYVHVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   88 AGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALhLPTQKIIRLYREECQFGYRDSVFK 167
Cdd:TIGR00179  80 GGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATIL-LATGKTEWLTNEQLGFGYRTSIFQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  168 HAMkndyvivaVGLRMAKQWKPVLTYGdlTKLNPATVCAWDIFNAICHMRQSKLPDPkitgNVGSFFKNPLitaehatal 247
Cdd:TIGR00179 159 HKY--------VGLVLKAEFQLTLGFG--TRLDPETITAQQVFNKVCRMRTSHYPDP----NAGSFFKNPS--------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  248 ikqwpaiPHYpqasgemklaAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEP 327
Cdd:TIGR00179 216 -------PNH----------AGRLIEECGLKGYQIGGAAVSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEP 278

                  ....*.
gi 495382281  328 EVRFIG 333
Cdd:TIGR00179 279 EVKIIG 284
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
5-333 4.76e-64

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 207.12  E-value: 4.76e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   5 NTSLEAFNTLGLAINAQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLED-FSGSVVVNAIKGITIEEHDEAwh 83
Cdd:PRK13903  18 DVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDgFDGTVVRVATRGVTVDCGGGL-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  84 LHVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALHLPTQKIIRLYREECQFGYRD 163
Cdd:PRK13903  96 VRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTITRVRLLDRRTGEVRWVPAADLGFGYRT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 164 SVFKHAMKndYVIVAV--GLRMAKQWKPVlTYGDLT---------KLNPATVCAwdifnAICHMRQSK---L-PDPKITG 228
Cdd:PRK13903 176 SVLKHSDR--AVVLEVefQLDPSGLSAPL-RYGELAralgvepgeRVPPAAVRE-----AVLALRAGKgmvLdPADHDTW 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 229 NVGSFFKNPLITAE-----HATALIKQWPAIPHYPQASGEMKLAAGWLIDQCGL-KGFRVGG--AAVHRQQALVLINENH 300
Cdd:PRK13903 248 SAGSFFTNPVVSPAvaerlAARVAERLGDPVPRYPAGDGGVKLSAAWLIERAGFgKGYPGGGapARLSTKHTLALTNRGG 327
                        330       340       350
                 ....*....|....*....|....*....|...
gi 495382281 301 ATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFIG 333
Cdd:PRK13903 328 ATTADLVALAREVRDGVRDAFGVTLVPEPVLVG 360
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
20-333 2.21e-52

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 174.91  E-value: 2.21e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  20 AQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLED-FSGSVVVNA--IKGITIEEHdeawHLHVGAGENWHALV 96
Cdd:PRK13905  31 ADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGgIRGVVIRLGkgLNEIEVEGN----RITAGAGAPLIKLA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  97 EQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALhLPTQKIIRLYREECQFGYRDSVFKhamKNDYVI 176
Cdd:PRK13905 107 RFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVL-DRDGEIKTLSNEELGFGYRHSALQ---EEGLIV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 177 VAVGLRmakqwkpvLTYGDLTKLNPATvcawdifNAICHMRQSKLP--DPkitgNVGSFFKNPLitaehatalikqwpai 254
Cdd:PRK13905 183 LSATFQ--------LEPGDKEEIKARM-------DELLARREATQPleYP----SAGSVFKNPP---------------- 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495382281 255 PHYpqasgemklaAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFIG 333
Cdd:PRK13905 228 GHF----------AGKLIEEAGLKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIG 296
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
209-332 2.00e-42

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: 142.49  E-value: 2.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  209 IFNAICHMRQSKL-PDPKITGNVGSFFKNPlitaehatalikqwpaIPHYpqasgemklaAGWLIDQCGLKGFRVGGAAV 287
Cdd:pfam02873   1 IRAAMLELRRRRLaKQPLDPPSAGSFFKNP----------------VGHS----------AGWLIEQAGLKGYRIGGAQV 54
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 495382281  288 HRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFI 332
Cdd:pfam02873  55 SEKHANFLVNTGGATAADVLALIEEVRERVKEKFGVELEPEVRII 99
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
46-329 8.17e-31

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 118.40  E-value: 8.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  46 FIVLGEGSNVLFLEDFSGSVVV--NAIKGITIEEHDeawhLHVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQ 123
Cdd:PRK14653  59 VKILGNGTNVLPKDEPMDFVVVstERLDDIFVDNDK----IICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYM 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 124 NIGAYGVEFKDICHYVEALHlpTQKIIRLYREECQFGYRDSVFKHamKNDYVIVAVGLRMAKqwkpvltyGDltklnpat 203
Cdd:PRK14653 135 NAGAYGWETAENIVEVVAYD--GKKIIRLGKNEIKFSYRNSIFKE--EKDLIILRVTFKLKK--------GN-------- 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 204 vcAWDIFNaicHMRQSKL----PDPKITGNVGSFFKNPlitaehatalikqwpaiphypqasgEMKLAAGWLIDQCGLKG 279
Cdd:PRK14653 195 --KNEIYN---LMLETMKkrveKQPLEFPSAGSVFKRP-------------------------RKDFYVGSAIEKLGLKG 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 495382281 280 FRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEV 329
Cdd:PRK14653 245 FSIGGAQISEKHAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEI 294
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
20-333 5.54e-30

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 116.09  E-value: 5.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  20 AQTLTIAETPD--AITLAWKNSQQLnqPFIVLGEGSNVLFL-EDFSGSVVVNAIKGITIEEHDEAWHLHVGAGENWHALV 96
Cdd:PRK14649  21 ARYFVEPTTPDeaIAAAAWAEQRQL--PLFWLGGGSNLLVRdEGFDGLVARYRGQRWELHEHGDTAEVWVEAGAPMAGTA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  97 EQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALhLPTQKIIRLYREECQFGYRDSVFKHaMKNDYVI 176
Cdd:PRK14649  99 RRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLL-LNGSECVEWSVHDFAYGYRTSVLKQ-LRADGIT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 177 VAVGLRMAKQWKpvLTYGDLTKLNPAtvcawdiFNAICHMRQSKLPdpkITGNVGSFFKNPlitaehatalikqwpaiph 256
Cdd:PRK14649 177 WRPPLVLAARFR--LHRDDPTALAAR-------MEAIAAERKQKTP---AGSSCGSVFKNP------------------- 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495382281 257 ypqaSGEmklAAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFIG 333
Cdd:PRK14649 226 ----PGD---SAGRLIEAAGLKGTRIGDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
30-333 3.76e-22

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 94.69  E-value: 3.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  30 DAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNA--IKGITIEehdeAWHLHVGAGENWHALVEQTLKKGITGL 107
Cdd:PRK12436  47 DEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIRGITVSLihITGVTVT----GTTIVAQCGAAIIDVSRIALDHNLTGL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 108 ENLALIPGMAGSAPIQNIGAYGVEFKDIchYVEALHLPTQ-KIIRLYREECQFGYRDSVFKHamkNDYVIVAVGLRMAKQ 186
Cdd:PRK12436 123 EFACGIPGSVGGALYMNAGAYGGEISFV--LTEAVVMTGDgELRTLTKEAFEFGYRKSVFAN---NHYIILEARFELEEG 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 187 wkpvlTYGDL-TKLNPATvcawdifnaicHMRQSKlpDPKITGNVGSFFKNPlitaehatalikqwpaiPHYpqasgemk 265
Cdd:PRK12436 198 -----VYEEIkAKMDDLT-----------FKRESK--QPLEYPSCGSVFKRP-----------------PNN-------- 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495382281 266 lAAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFIG 333
Cdd:PRK12436 235 -FAGKLIQESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIG 301
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
25-152 8.46e-21

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: 86.87  E-value: 8.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   25 IAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVN--AIKGItIEEHDEAWHLHVGAGENWHALVEQTLKK 102
Cdd:pfam01565   6 LPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDlsRLNGI-LEIDPEDGTATVEAGVTLGDLVRALAAK 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495382281  103 G-ITGLENLALIPGMAGSAPIQNIGAYGVEF----KDICHYVEALhLPTQKIIRL 152
Cdd:pfam01565  85 GlLLGLDPGSGIPGTVGGAIATNAGGYGSEKygltRDNVLGLEVV-LADGEVVRL 138
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
8-326 2.23e-20

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 89.11  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281   8 LEAFNTLGLAINAQTLTIaETPDAITLAwknsqqLNQPFIVLGEGSNVLFLEDFSGSVVVNaIKGITIEEHDEAWhlhVG 87
Cdd:PRK14651   9 LARYTTLGVGGPAELWTV-ETHEQLAEA------TEAPYRVLGGGSNLLVSDAGVPERVIR-LGGEFAEWDLDGW---VG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  88 AGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEALHlpTQKIIRLYREECQFGYRDSvfk 167
Cdd:PRK14651  78 GGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVH--DGGFHQYSPDELGFGYRHS--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 168 hAMKNDYVIVAVGLRmakqwkpvltygdLTKLNPATVCAwdifnAICHMRQSKLPDPKITgNVGSFFKNPlitaehatal 247
Cdd:PRK14651 153 -GLPPGHVVTRVRLK-------------LRPSTPEAVLA-----KMALVDAARKGQPKKK-SAGCAFKNP---------- 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 248 ikqwpaiphyPQASgemklaAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVG----QKFDV 323
Cdd:PRK14651 203 ----------PGDS------AGRLIDEAGLKGTRVGDAMISPEHGNFIVNLGGATAADVHALLRRVRARVGlpleLEWEL 266

                 ...
gi 495382281 324 WLE 326
Cdd:PRK14651 267 WPE 269
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
39-333 8.53e-20

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 88.34  E-value: 8.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  39 SQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITIEEHDEAwhLHVGAGENWHALVEQTLKKGITGLENLALIPGMAG 118
Cdd:PRK13906  56 AYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDDA--IIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 119 SAPIQNIGAYGVEFKDICHYveALHLPTQ-KIIRLYREECQFGYRDSVFKhamKNDYVIVAVGLRMAKqwkpvltyGDLT 197
Cdd:PRK13906 134 GAVYMNAGAYGGEVKDCIDY--ALCVNEQgSLIKLTTKELELDYRNSIIQ---KEHLVVLEAAFTLAP--------GKMT 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 198 KLNPAtvcawdiFNAICHMRQSKlpDPKITGNVGSFFKNPlitaehatalikqwPAipHYpqasgemklaAGWLIDQCGL 277
Cdd:PRK13906 201 EIQAK-------MDDLTERRESK--QPLEYPSCGSVFQRP--------------PG--HF----------AGKLIQDSNL 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495382281 278 KGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFIG 333
Cdd:PRK13906 246 QGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
83-329 1.87e-17

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 80.74  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  83 HLHVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDICHYVEalhlpTQKIIRLyREECQFGYR 162
Cdd:PRK13904  68 CLEIGGATKSGKIFNYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLESIC-----TNGGWIE-KEDIGFGYR 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 163 DSVFKHamkndyVIVAVGLRmakqwkpvLTYGDLTKLNpatvcawDIFNAichMRQSKlpdPKiTGNVGSFFKNPlitae 242
Cdd:PRK13904 142 SSGING------VILEARFK--------KTHGFDEELL-------EAFKS---MRKNQ---PK-GPSFGSCFKNP----- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 243 hatalikqwpaIPHYpqasgemklaAGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFD 322
Cdd:PRK13904 189 -----------KGDY----------AGRLIEAVGLKGYCKGGAGFSEEHANFLVNLGGATFEDALDLIELAKKRVLEEFG 247

                 ....*..
gi 495382281 323 VWLEPEV 329
Cdd:PRK13904 248 INLEEEV 254
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
20-333 1.99e-17

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 81.46  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  20 AQTLTIAETPDAITLAWKNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITIEEHDEAwHLHVGAGENWHALVEQT 99
Cdd:PRK14652  36 ADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGESTDGG-RLVLGAGAPISRLPARA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 100 LKKGITGLENLALIPGMAGSAPIQNIGAYGVEFKDIchyVEALHLPTQKIIR-LYREECQFGYRDSvfkhAMKNDYVIVA 178
Cdd:PRK14652 115 HAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDV---VTAVELATADGAGfVPAAALGYAYRTC----RLPPGAVITR 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 179 VGLRMAKqwkpvltyGDLtklnpatVCAWDIFNAICHMRQSKLPDPKitGNVGSFFKNPliTAEHAtalikqwpaiphyp 258
Cdd:PRK14652 188 VEVRLRP--------GDV-------AASEALMRADRERRRRTQPLDR--PTFGSTFTNP--PGDYA-------------- 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495382281 259 qasgemklaaGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFIG 333
Cdd:PRK14652 235 ----------GRLVEAVGLKGHRVGGAIWSPVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLG 299
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
37-333 3.99e-10

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 60.51  E-value: 3.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  37 KNSQQLNQPFIVLGEGSNVLFLEDFSGSVVVNAIKGITIE---EHDEAWHLHVGAGENWHALVEQTLKKGITGLENLALI 113
Cdd:PRK14648  47 EEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRRFRSLHtqtQRDGSVLVHAGAGLPVAALLAFCAHHALRGLETFAGL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 114 PGMAGSAPIQNIGAYGVEFKDICHYVEAL----------HLP-TQKIIRLYREEC---------------------QFGY 161
Cdd:PRK14648 127 PGSVGGAAYMNARCYGRAIADCFHSARTLvlhpvrsrakELPeVRKNAQDKRGEClgldggpftcssfqtvfaragDWGY 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 162 RDSVFKHAMKndyVIVAVGLRMAKQWKPVLTYGdltklNPATVCAwdifnaicHMrQSKLPDPKITG-----NVGSFFKN 236
Cdd:PRK14648 207 KRSPFQSPHG---VELHAGRRLILSLCVRLTPG-----NPAQIRK--------HM-QEKIADRISKGqfrfpSAGSAFKN 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 237 PlitaehatalikqwpaiPHYPQASgemklaaGWLIDQCGLKGFRVGGAAVHRQQALVLINENHATPQDIVDLAHLVRDR 316
Cdd:PRK14648 270 N-----------------PAFGKPS-------GILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQR 325
                        330
                 ....*....|....*..
gi 495382281 317 VGQKFDVWLEPEVRFIG 333
Cdd:PRK14648 326 VFETHGVWLEREIIFSG 342
PRK14650 PRK14650
UDP-N-acetylmuramate dehydrogenase;
48-333 6.17e-10

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173113 [Multi-domain]  Cd Length: 302  Bit Score: 59.47  E-value: 6.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281  48 VLGEGSNVLFLEDFSGSVVVNAIKGIT-IEEHDEawHLHVGAGENWHALVEQTLKKGITGLENLALIPGMAGSAPIQNIG 126
Cdd:PRK14650  61 ILGGGSNILINDEEEIDFPIIYTGHLNkIEIHDN--QIVAECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNAR 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 127 AYGVEFKDICHYVEALHLPTQKIIRLYREEcQFGYRDSVFKHamKNdYVIVAVGLRMAKQWKPVLTygdltklnpatvca 206
Cdd:PRK14650 139 CFGNEISEILDKITFIDEKGKTICKKFKKE-EFKYKISPFQN--KN-TFILKATLNLKKGNKKHIE-------------- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495382281 207 wDIFNAICHMRQSKlpDPKITGNVGSFFKNplitaehATALIKqwpaiphypqasgemklAAGWLIDQCGLKGFRVGGAA 286
Cdd:PRK14650 201 -EIMKQNKQIRINK--GHYLFPSSGSTFKN-------NKAFLK-----------------PTGQIIEECKLKGLSIGGAT 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 495382281 287 VHRQQALVLINENHATPQDIVDLAHLVRDRVGQKFDVWLEPEVRFIG 333
Cdd:PRK14650 254 VSHYHGNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
 
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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