NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2116813794|gb|UCU95819|]
View 

UDP-N-acetylmuramate dehydrogenase [Hydrogenophaga taeniospiralis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
1-349 0e+00

UDP-N-acetylmuramate dehydrogenase;


:

Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 543.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   1 MLVENNVALQPLNSFGIAARAQRFARVRSEADLTGLMNGPDWAA-PVFVLGGGSNLVITGDIKALVLKVDIPGRRLVEET 79
Cdd:PRK00046    1 MQLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGlPVLVLGGGSNVLFTEDFDGTVLLNRIKGIEVLSED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  80 AKGWVVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDLQSGRAFTLDAAQCG 159
Cdd:PRK00046   81 DDAWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDYVEALDLATGEFVRLSAAECR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 160 FGYRDSVFKHvptdarsfGLAGRALITRVRFLLPKPWKPVLGYLDLERKMAetgiHTPDAQQIFDWVVAIRRAKLPDPAV 239
Cdd:PRK00046  161 FGYRDSIFKH--------EYPDRYAITAVGFRLPKQWQPVLDYGDLARLDP----DTVTAQDVFDAVCAIRRSKLPDPKV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 240 IGNAGSFFKNPTVTPEQCADIIARDPKVVHYPMPDGSIKLAAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCT 319
Cdd:PRK00046  229 LGNAGSFFKNPVVSAEQFEALLAQYPDIPHYPQADGSVKLAAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGN----AT 304
                         330       340       350
                  ....*....|....*....|....*....|
gi 2116813794 320 GGEVMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:PRK00046  305 GADVLALARHIQQDVREKFGVELEPEPRFI 334
 
Name Accession Description Interval E-value
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
1-349 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 543.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   1 MLVENNVALQPLNSFGIAARAQRFARVRSEADLTGLMNGPDWAA-PVFVLGGGSNLVITGDIKALVLKVDIPGRRLVEET 79
Cdd:PRK00046    1 MQLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGlPVLVLGGGSNVLFTEDFDGTVLLNRIKGIEVLSED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  80 AKGWVVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDLQSGRAFTLDAAQCG 159
Cdd:PRK00046   81 DDAWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDYVEALDLATGEFVRLSAAECR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 160 FGYRDSVFKHvptdarsfGLAGRALITRVRFLLPKPWKPVLGYLDLERKMAetgiHTPDAQQIFDWVVAIRRAKLPDPAV 239
Cdd:PRK00046  161 FGYRDSIFKH--------EYPDRYAITAVGFRLPKQWQPVLDYGDLARLDP----DTVTAQDVFDAVCAIRRSKLPDPKV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 240 IGNAGSFFKNPTVTPEQCADIIARDPKVVHYPMPDGSIKLAAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCT 319
Cdd:PRK00046  229 LGNAGSFFKNPVVSAEQFEALLAQYPDIPHYPQADGSVKLAAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGN----AT 304
                         330       340       350
                  ....*....|....*....|....*....|
gi 2116813794 320 GGEVMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:PRK00046  305 GADVLALARHIQQDVREKFGVELEPEPRFI 334
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
7-349 2.97e-119

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: 345.46  E-value: 2.97e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   7 VALQPLNSFGIAARAQRFARVRSEADLTGLMNGPDWAA-PVFVLGGGSNLVITGD-IKALVLKV-DIPGRRLVEetakGW 83
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGlPVLVLGGGSNLLVRDDgFDGLVIRLgRLKGIEVDD----GV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  84 VVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDlQSGRAFTLDAAQCGFGYR 163
Cdd:COG0812    77 LVTAGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLD-RTGEVRTLSAEECGFGYR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 164 DSVFKHvptdarsfglaGRALITRVRFLLPKpwkpvlgyldlerkmaetgiHTPDA-QQIFDWVVAIRRAKlpDPAVIGN 242
Cdd:COG0812   156 DSIFKR-----------ERYIILSVTFRLKK--------------------GDPAEiAAVMDAVLAIRRSK--QPLELPS 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 243 AGSFFKNPtvtpeqcadiiardpkvvhypmPDGSiklaAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGE 322
Cdd:COG0812   203 AGSFFKNP----------------------PGDS----AGWLIEQAGLKGYRIGGAQVSEKHANFLVNRGG----ATAAD 252
                         330       340
                  ....*....|....*....|....*..
gi 2116813794 323 VMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:COG0812   253 VLALIEEVQARVKEKFGVELEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
9-345 1.66e-73

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: 229.26  E-value: 1.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   9 LQPLNSFGIAARAQRFARVRSEADLTGLMngpDWAA----PVFVLGGGSNLVITGDIKALVLKVDIPGRRLVEEtaKGWV 84
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVL---DNAKeedqPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDD--EGEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  85 VEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDaIDLQSGRAFTLDAAQCGFGYRD 164
Cdd:TIGR00179  76 VHVGGGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYAT-ILLATGKTEWLTNEQLGFGYRT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 165 SVFKHvptdarsfglagraliTRVRFLLPKPWKPVLGYldleRKMAETGIHTpdAQQIFDWVVAIRRAKLPDPavigNAG 244
Cdd:TIGR00179 155 SIFQH----------------KYVGLVLKAEFQLTLGF----GTRLDPETIT--AQQVFNKVCRMRTSHYPDP----NAG 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 245 SFFKNPTVTPeqcadiiardpkvvhypmpdgsiklaAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGEVM 324
Cdd:TIGR00179 209 SFFKNPSPNH--------------------------AGRLIEECGLKGYQIGGAAVSKQHANFLVNIDN----AKSEDVL 258
                         330       340
                  ....*....|....*....|.
gi 2116813794 325 TLAKAIQTSVYERFGIRLEPE 345
Cdd:TIGR00179 259 DLIEHVKAEVGEKYGILLEPE 279
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
222-349 8.96e-40

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: 135.94  E-value: 8.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 222 IFDWVVAIRRAKL-PDPAVIGNAGSFFKNPtvtpeqcadiiardpkvvhypmpdgsIKLAAGWLIDACGWKGKSVGNAAV 300
Cdd:pfam02873   1 IRAAMLELRRRRLaKQPLDPPSAGSFFKNP--------------------------VGHSAGWLIEQAGLKGYRIGGAQV 54
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2116813794 301 YEKQALVLVNRGGpshpCTGGEVMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:pfam02873  55 SEKHANFLVNTGG----ATAADVLALIEEVRERVKEKFGVELEPEVRII 99
 
Name Accession Description Interval E-value
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
1-349 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 543.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   1 MLVENNVALQPLNSFGIAARAQRFARVRSEADLTGLMNGPDWAA-PVFVLGGGSNLVITGDIKALVLKVDIPGRRLVEET 79
Cdd:PRK00046    1 MQLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGlPVLVLGGGSNVLFTEDFDGTVLLNRIKGIEVLSED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  80 AKGWVVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDLQSGRAFTLDAAQCG 159
Cdd:PRK00046   81 DDAWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDYVEALDLATGEFVRLSAAECR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 160 FGYRDSVFKHvptdarsfGLAGRALITRVRFLLPKPWKPVLGYLDLERKMAetgiHTPDAQQIFDWVVAIRRAKLPDPAV 239
Cdd:PRK00046  161 FGYRDSIFKH--------EYPDRYAITAVGFRLPKQWQPVLDYGDLARLDP----DTVTAQDVFDAVCAIRRSKLPDPKV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 240 IGNAGSFFKNPTVTPEQCADIIARDPKVVHYPMPDGSIKLAAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCT 319
Cdd:PRK00046  229 LGNAGSFFKNPVVSAEQFEALLAQYPDIPHYPQADGSVKLAAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGN----AT 304
                         330       340       350
                  ....*....|....*....|....*....|
gi 2116813794 320 GGEVMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:PRK00046  305 GADVLALARHIQQDVREKFGVELEPEPRFI 334
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
7-349 2.97e-119

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: 345.46  E-value: 2.97e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   7 VALQPLNSFGIAARAQRFARVRSEADLTGLMNGPDWAA-PVFVLGGGSNLVITGD-IKALVLKV-DIPGRRLVEetakGW 83
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGlPVLVLGGGSNLLVRDDgFDGLVIRLgRLKGIEVDD----GV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  84 VVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDlQSGRAFTLDAAQCGFGYR 163
Cdd:COG0812    77 LVTAGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLD-RTGEVRTLSAEECGFGYR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 164 DSVFKHvptdarsfglaGRALITRVRFLLPKpwkpvlgyldlerkmaetgiHTPDA-QQIFDWVVAIRRAKlpDPAVIGN 242
Cdd:COG0812   156 DSIFKR-----------ERYIILSVTFRLKK--------------------GDPAEiAAVMDAVLAIRRSK--QPLELPS 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 243 AGSFFKNPtvtpeqcadiiardpkvvhypmPDGSiklaAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGE 322
Cdd:COG0812   203 AGSFFKNP----------------------PGDS----AGWLIEQAGLKGYRIGGAQVSEKHANFLVNRGG----ATAAD 252
                         330       340
                  ....*....|....*....|....*..
gi 2116813794 323 VMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:COG0812   253 VLALIEEVQARVKEKFGVELEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
9-345 1.66e-73

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: 229.26  E-value: 1.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   9 LQPLNSFGIAARAQRFARVRSEADLTGLMngpDWAA----PVFVLGGGSNLVITGDIKALVLKVDIPGRRLVEEtaKGWV 84
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVL---DNAKeedqPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDD--EGEY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  85 VEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDaIDLQSGRAFTLDAAQCGFGYRD 164
Cdd:TIGR00179  76 VHVGGGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYAT-ILLATGKTEWLTNEQLGFGYRT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 165 SVFKHvptdarsfglagraliTRVRFLLPKPWKPVLGYldleRKMAETGIHTpdAQQIFDWVVAIRRAKLPDPavigNAG 244
Cdd:TIGR00179 155 SIFQH----------------KYVGLVLKAEFQLTLGF----GTRLDPETIT--AQQVFNKVCRMRTSHYPDP----NAG 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 245 SFFKNPTVTPeqcadiiardpkvvhypmpdgsiklaAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGEVM 324
Cdd:TIGR00179 209 SFFKNPSPNH--------------------------AGRLIEECGLKGYQIGGAAVSKQHANFLVNIDN----AKSEDVL 258
                         330       340
                  ....*....|....*....|.
gi 2116813794 325 TLAKAIQTSVYERFGIRLEPE 345
Cdd:TIGR00179 259 DLIEHVKAEVGEKYGILLEPE 279
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
6-349 2.77e-73

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 231.00  E-value: 2.77e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   6 NVALQPLNSFGIAARAQRFARVRSEADLTGLMNGPDWAA-PVFVLGGGSNLVITGDIKAL-VLKVDIPGRRLVEETAkgw 83
Cdd:PRK13903   18 DVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGePLLVLGGGSNLVIADDGFDGtVVRVATRGVTVDCGGG--- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  84 VVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDLQSGRAFTLDAAQCGFGYR 163
Cdd:PRK13903   95 LVRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTITRVRLLDRRTGEVRWVPAADLGFGYR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 164 DSVFKHvptdarsfglAGRALITRVRF-LLPKPWKPVLGYLDLERKM-AETGIHTPdAQQIFDWVVAIRRAK--LPDPA- 238
Cdd:PRK13903  175 TSVLKH----------SDRAVVLEVEFqLDPSGLSAPLRYGELARALgVEPGERVP-PAAVREAVLALRAGKgmVLDPAd 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 239 -VIGNAGSFFKNPTVTPEQCADIIAR-----DPKVVHYPMPDGSIKLAAGWLID----ACGWKGKSvGNAAVYEKQALVL 308
Cdd:PRK13903  244 hDTWSAGSFFTNPVVSPAVAERLAARvaerlGDPVPRYPAGDGGVKLSAAWLIEragfGKGYPGGG-APARLSTKHTLAL 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2116813794 309 VNRGGpshpCTGGEVMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:PRK13903  323 TNRGG----ATTADLVALAREVRDGVRDAFGVTLVPEPVLV 359
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
6-345 1.71e-49

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 167.60  E-value: 1.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   6 NVALQPLNSFGIAARAQRFARVRSEADLTGLMNG-PDWAAPVFVLGGGSNLVIT-GDIKALVLKVdipGRRLVEETAKGW 83
Cdd:PRK13905   16 NEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLlKENNIPVTVLGNGSNLLVRdGGIRGVVIRL---GKGLNEIEVEGN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  84 VVEAGAGENwHQFVAWTLV-QGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDlQSGRAFTLDAAQCGFGY 162
Cdd:PRK13905   93 RITAGAGAP-LIKLARFAAeAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLD-RDGEIKTLSNEELGFGY 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 163 RDSVFKhvptdarsfglAGRALITRVRFLLPKpwkpvlG-YLDLERKMAEtgihtpdaqqifdwVVAIRRAKLP--DPav 239
Cdd:PRK13905  171 RHSALQ-----------EEGLIVLSATFQLEP------GdKEEIKARMDE--------------LLARREATQPleYP-- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 240 igNAGSFFKNPTVtpeqcadiiardpkvvHYpmpdgsiklaAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCT 319
Cdd:PRK13905  218 --SAGSVFKNPPG----------------HF----------AGKLIEEAGLKGYRIGGAQVSEKHANFIINTGG----AT 265
                         330       340
                  ....*....|....*....|....*.
gi 2116813794 320 GGEVMTLAKAIQTSVYERFGIRLEPE 345
Cdd:PRK13905  266 AADIEDLIEHVQKTVKEKFGVELEWE 291
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
222-349 8.96e-40

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: 135.94  E-value: 8.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 222 IFDWVVAIRRAKL-PDPAVIGNAGSFFKNPtvtpeqcadiiardpkvvhypmpdgsIKLAAGWLIDACGWKGKSVGNAAV 300
Cdd:pfam02873   1 IRAAMLELRRRRLaKQPLDPPSAGSFFKNP--------------------------VGHSAGWLIEQAGLKGYRIGGAQV 54
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2116813794 301 YEKQALVLVNRGGpshpCTGGEVMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:pfam02873  55 SEKHANFLVNTGG----ATAADVLALIEEVRERVKEKFGVELEPEVRII 99
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
9-349 7.52e-25

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 102.23  E-value: 7.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   9 LQPLNSFGIAARAQRFARVRSEADLTGLMNgpdWAA----PVFVLGGGSNLVITGD-IKALVLKVDIPGRRLVE--ETAK 81
Cdd:PRK14649    9 LAPYTSWRIGGPARYFVEPTTPDEAIAAAA---WAEqrqlPLFWLGGGSNLLVRDEgFDGLVARYRGQRWELHEhgDTAE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  82 GWVvEAGAGenwhqfVAWTL----VQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIdLQSGRAFTLDAAQ 157
Cdd:PRK14649   86 VWV-EAGAP------MAGTArrlaAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLL-LNGSECVEWSVHD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 158 CGFGYRDSVFKHVPTDarsfGLAGR-ALITRVRFLLPKPwKPVLgyldLERKMAETGihtpdaqqifdwvvAIRRAKLPD 236
Cdd:PRK14649  158 FAYGYRTSVLKQLRAD----GITWRpPLVLAARFRLHRD-DPTA----LAARMEAIA--------------AERKQKTPA 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 237 PAvigNAGSFFKNPTVTpeqcadiiardpkvvhypmpdgsiklAAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpsh 316
Cdd:PRK14649  215 GS---SCGSVFKNPPGD--------------------------SAGRLIEAAGLKGTRIGDAEIATRHANYIINLGG--- 262
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2116813794 317 pCTGGEVMTLAKAIQTSVYERFGIRLEPEPVVV 349
Cdd:PRK14649  263 -ARAADILRLIDLARTRVLAQFGIELELEVRII 294
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
7-345 5.98e-18

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 82.56  E-value: 5.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   7 VALQPLNSFGIAARAQRFArVRSEADLTGLMNgpdwaAPVFVLGGGSNLVITGD-IKALVLKVdipGRRLVEETAKGWVv 85
Cdd:PRK14651    7 VPLARYTTLGVGGPAELWT-VETHEQLAEATE-----APYRVLGGGSNLLVSDAgVPERVIRL---GGEFAEWDLDGWV- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  86 eaGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAidLQSGRAFTLDAAQCGFGYRDS 165
Cdd:PRK14651   77 --GGGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEI--VHDGGFHQYSPDELGFGYRHS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 166 vfkhvptdarsfGLAGRALITRVRF-LLPKPWKPVLgyldleRKMAEtgihtpdaqqifdwVVAIRRAKlPDPAvigNAG 244
Cdd:PRK14651  153 ------------GLPPGHVVTRVRLkLRPSTPEAVL------AKMAL--------------VDAARKGQ-PKKK---SAG 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 245 SFFKNPtvtpeqcadiiardPKVvhypmpdgsiklAAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGEVM 324
Cdd:PRK14651  197 CAFKNP--------------PGD------------SAGRLIDEAGLKGTRVGDAMISPEHGNFIVNLGG----ATAADVH 246
                         330       340
                  ....*....|....*....|.
gi 2116813794 325 TLAKAIQtsvyERFGIRLEPE 345
Cdd:PRK14651  247 ALLRRVR----ARVGLPLELE 263
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
21-144 6.09e-17

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: 76.47  E-value: 6.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  21 AQRFARVRSEADLTGLMNgpdWAA----PVFVLGGGSNLV-ITGDIKALVLKVDiPGRRLVEETAKGWVVEAGAGENWHQ 95
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVR---LANenglPVLPRGGGSSLLgGAVQTGGIVLDLS-RLNGILEIDPEDGTATVEAGVTLGD 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2116813794  96 FVAWTLVQG-WPGLENLALIPGSVGASPVQNIGAYGVELQ----DRFHSLDAID 144
Cdd:pfam01565  77 LVRALAAKGlLLGLDPGSGIPGTVGGAIATNAGGYGSEKYgltrDNVLGLEVVL 130
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
85-345 1.72e-16

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 78.72  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  85 VEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDlqSGRAFTLDAAQCGFGYRD 164
Cdd:PRK14653   95 IICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVEVVAYD--GKKIIRLGKNEIKFSYRN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 165 SVFKHvptdarsfglAGRALITRVRFLLPKPWKpvlgYLDLERkMAETGIHTPDAQqifdwvvairraklpdPAVIGNAG 244
Cdd:PRK14653  173 SIFKE----------EKDLIILRVTFKLKKGNK----NEIYNL-MLETMKKRVEKQ----------------PLEFPSAG 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 245 SFFKNPTvtpeqcadiiardpkvvhypmPDgsikLAAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGEVM 324
Cdd:PRK14653  222 SVFKRPR---------------------KD----FYVGSAIEKLGLKGFSIGGAQISEKHAGFIINYNN----AKAEDVL 272
                         250       260
                  ....*....|....*....|.
gi 2116813794 325 TLAKAIQTSVYERFGIRLEPE 345
Cdd:PRK14653  273 KLIEYVKDKIYENYNVELETE 293
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
9-345 1.02e-14

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 73.75  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   9 LQPLNSFGIAARAQRFARVRSEADLTGLMNGP-DWAAPVFVLGGGSN-LVITGDIKALVLKvdIPGRrLVEETAKGWVVE 86
Cdd:PRK14652   24 LAPRTAVRVGGPADLLVRPADPDALSALLRAVrELGVPLSILGGGANtLVADAGVRGVVLR--LPQD-FPGESTDGGRLV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  87 AGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDaIDLQSGRAFtLDAAQCGFGYRDSv 166
Cdd:PRK14652  101 LGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVTAVE-LATADGAGF-VPAAALGYAYRTC- 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 167 fkhvptdarsfGLAGRALITRVRFLLPKPwkpvlgyldlerkmaetgiHTPDAQQIFDWVVAIRRAKlpDPAVIGNAGSF 246
Cdd:PRK14652  178 -----------RLPPGAVITRVEVRLRPG-------------------DVAASEALMRADRERRRRT--QPLDRPTFGST 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 247 FKNPtvtPEQcadiiardpkvvhypmpdgsiklAAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGEVMTL 326
Cdd:PRK14652  226 FTNP---PGD-----------------------YAGRLVEAVGLKGHRVGGAIWSPVHANFVTNLGG----ATARDVLAL 275
                         330
                  ....*....|....*....
gi 2116813794 327 AKAIQTSVYERFGIRLEPE 345
Cdd:PRK14652  276 VRLARARVKERFGIALETE 294
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
107-349 4.23e-12

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 65.33  E-value: 4.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 107 GLENLALIPGSVGASPVQNIGAYGVELqdrFHSLDAIDLQSGRaftLDAAQCGFGYRDSVFKHVptdarsfglagralIT 186
Cdd:PRK13904   91 GFEFLGKLPGTLGGLVKMNAGLKEYEI---SNNLESICTNGGW---IEKEDIGFGYRSSGINGV--------------IL 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 187 RVRFLLPKPWKPVLgyLDLERKMaetgihtpdaqqifdwvvairRAKLPDPAvigNAGSFFKNPtvtpeqcadiiardpk 266
Cdd:PRK13904  151 EARFKKTHGFDEEL--LEAFKSM---------------------RKNQPKGP---SFGSCFKNP---------------- 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 267 VVHYpmpdgsiklaAGWLIDACGWKGKSVGNAAVYEKQALVLVNRGGPSHpCTGGEVMTLAKAiqtSVYERFGIRLEPEP 346
Cdd:PRK13904  189 KGDY----------AGRLIEAVGLKGYCKGGAGFSEEHANFLVNLGGATF-EDALDLIELAKK---RVLEEFGINLEEEV 254

                  ...
gi 2116813794 347 VVV 349
Cdd:PRK13904  255 IIL 257
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
45-345 7.29e-12

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 65.42  E-value: 7.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  45 PVFVLGGGSNLVIT-GDIKALVLKVdipgRRLVEETAKGWVVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPV 123
Cdd:PRK12436   62 PVTFLGNGSNVIIKdGGIRGITVSL----IHITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALY 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 124 QNIGAYGVELQdrFHSLDAIDL-QSGRAFTLDAAQCGFGYRDSVFKHvptdarsfglaGRALITRVRFLLPKPwkpvlGY 202
Cdd:PRK12436  138 MNAGAYGGEIS--FVLTEAVVMtGDGELRTLTKEAFEFGYRKSVFAN-----------NHYIILEARFELEEG-----VY 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 203 LDLERKMaetgihtpdaqqifDWVVAIRRAKLPdpavignagsfFKNPTvtpeqCADIIARDPKvvHYpmpdgsiklaAG 282
Cdd:PRK12436  200 EEIKAKM--------------DDLTFKRESKQP-----------LEYPS-----CGSVFKRPPN--NF----------AG 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2116813794 283 WLIDACGWKGKSVGNAAVYEKQALVLVNRGGPshpcTGGEVMTLAKAIQTSVYERFGIRLEPE 345
Cdd:PRK12436  238 KLIQESGLQGKRIGGVEVSLKHAGFMVNVDNG----TAQDYIDLIHFVQKTVEEKFGVKLERE 296
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
2-345 2.84e-11

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 63.97  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794   2 LVENNVALQPLNSFGIAARAQRFARVRSEADLTGLMNGPDWA-APVFVLGGGSNLVITGD-IKALVLKVDiPGRRLVEET 79
Cdd:PRK14648   11 ITRRNVPLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRArIPLSLIGGGSNVLIADEgVPGLMLSLR-RFRSLHTQT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  80 AK--GWVVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPVQNIGAYGVELQDRFHSLDAIDLQSGRA------- 150
Cdd:PRK14648   90 QRdgSVLVHAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARTLVLHPVRSrakelpe 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 151 -------------------FTLDAAQCGF------GYRDSVFKHvPTDARSFglAGRALITRVRFLLpKPWKPVLGYLDL 205
Cdd:PRK14648  170 vrknaqdkrgeclgldggpFTCSSFQTVFaragdwGYKRSPFQS-PHGVELH--AGRRLILSLCVRL-TPGNPAQIRKHM 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 206 ERKMAETgihtpdaqqifdwvvaIRRAKLPDPAvignAGSFFKNptvtpeqcadiiardpkvvhypmpDGSIKLAAGWLI 285
Cdd:PRK14648  246 QEKIADR----------------ISKGQFRFPS----AGSAFKN------------------------NPAFGKPSGILI 281
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 286 DACGWKGKSVGNAAVYEKQALVLVNRGGpshpCTGGEVMTLAKAIQTSVYERFGIRLEPE 345
Cdd:PRK14648  282 EEAGLRGTSCGAAQVAPWHGNLIINTGN----ATAHQVRTLLRVVRQRVFETHGVWLERE 337
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
45-345 6.55e-07

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 50.20  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794  45 PVFVLGGGSNLVI-TGDIKALVLKVDIPGRRLVEETAkgwvVEAGAGENWHQFVAWTLVQGWPGLENLALIPGSVGASPV 123
Cdd:PRK13906   62 PVTYLGNGSNIIIrEGGIRGIVISLLSLDHIEVSDDA----IIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVY 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 124 QNIGAYGVELQDRFHSLDAIDlQSGRAFTLDAAQCGFGYRDSVF--KHVPTDARSFGLAGralitrvrfllpkpwkpvlG 201
Cdd:PRK13906  138 MNAGAYGGEVKDCIDYALCVN-EQGSLIKLTTKELELDYRNSIIqkEHLVVLEAAFTLAP-------------------G 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116813794 202 YLDlerkmaetgihtpDAQQIFDWVVAIRRAKLPdpavignagsfFKNPTvtpeqCADIIARDPKvvHYpmpdgsiklaA 281
Cdd:PRK13906  198 KMT-------------EIQAKMDDLTERRESKQP-----------LEYPS-----CGSVFQRPPG--HF----------A 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2116813794 282 GWLIDACGWKGKSVGNAAVYEKQA--LVLVNRGgpshpcTGGEVMTLAKAIQTSVYERFGIRLEPE 345
Cdd:PRK13906  237 GKLIQDSNLQGHRIGGVEVSTKHAgfMVNVDNG------TATDYENLIHYVQKTVKEKFGIELNRE 296
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH