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Conserved domains on  [gi|1327556126|gb|PMP93397|]
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MAG: UDP-N-acetylenolpyruvoylglucosamine reductase [Hydrogenobaculum sp.]

Protein Classification

UDP-N-acetylmuramate dehydrogenase( domain architecture ID 11435281)

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 COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 7-280 4.74e-92

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: 273.43  E-value: 4.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   7 VDLRDFTTIKIGGVGSYMFFPENEKEFLDIYK--KHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIKISEtkeGIL 82
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRaaREAGLPVLVLGGGSNLLVRDdgFDGLVIRLGRLKGIEVDD---GVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  83 VKASAGVPLKDLIKLSVENNVE--EFykLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIFYTYR 159
Cdd:COG0812    78 VTAGAGENWHDLVRFALEAGLSglEF--LAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTgEVRTLSAEECGFGYR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 160 KTEFENKP--VLYGEF-LFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFS 236
Cdd:COG0812   156 DSIFKRERyiILSVTFrLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVS 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1327556126 237 QKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:COG0812   236 EKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
 
Name Accession Description Interval E-value
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 7-280 4.74e-92

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: 273.43  E-value: 4.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   7 VDLRDFTTIKIGGVGSYMFFPENEKEFLDIYK--KHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIKISEtkeGIL 82
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRaaREAGLPVLVLGGGSNLLVRDdgFDGLVIRLGRLKGIEVDD---GVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  83 VKASAGVPLKDLIKLSVENNVE--EFykLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIFYTYR 159
Cdd:COG0812    78 VTAGAGENWHDLVRFALEAGLSglEF--LAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTgEVRTLSAEECGFGYR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 160 KTEFENKP--VLYGEF-LFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFS 236
Cdd:COG0812   156 DSIFKRERyiILSVTFrLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVS 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1327556126 237 QKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:COG0812   236 EKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
5-280 7.14e-77

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 235.78  E-value: 7.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   5 KNVDLRDFTTIKIGGVGSYMFFPENE---KEFLDIYKKHkNDKLCILGKGSNTIFGD--FNG-VLINTKHFYDIKISETK 78
Cdd:PRK13905   15 ENEPLARYTSFRVGGPADYLVEPADIedlQEFLKLLKEN-NIPVTVLGNGSNLLVRDggIRGvVIRLGKGLNEIEVEGNR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  79 egilVKASAGVPLKDLIKLSVENNVE--EFykLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIF 155
Cdd:PRK13905   94 ----ITAGAGAPLIKLARFAAEAGLSglEF--AAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDgEIKTLSNEELG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 156 YTYRKTEFENKP--VLYGEF-LFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKD 232
Cdd:PRK13905  168 FGYRHSALQEEGliVLSATFqLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLKGYRIGG 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1327556126 233 IGFSQKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:PRK13905  248 AQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRII 295
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 9-280 1.31e-56

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: 183.42  E-value: 1.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   9 LRDFTTIKIGGVGSYMFFPENEKEFLDIYK--KHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIKISEtkeGILVK 84
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDnaKEEDQPLLILGEGSNLLILDdgRGGVIINLGKGIDIEDDE---GEYVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  85 ASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIFYTYRKTEF 163
Cdd:TIGR00179  78 VGGGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATgKTEWLTNEQLGFGYRTSIF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 164 ENKPV---------LYGEFLFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIG 234
Cdd:TIGR00179 158 QHKYVglvlkaefqLTLGFGTRLDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAA 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1327556126 235 FSQKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:TIGR00179 238 VSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKII 283
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 187-280 6.22e-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: 134.40  E-value: 6.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 187 QTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFSQKHANFLINYQNASFQNVIDILSIAKERVY 266
Cdd:pfam02873   6 LELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEVRERVK 85

                          90
                  ....*....|....
gi 1327556126 267 KAFNIILEEEIKLV 280
Cdd:pfam02873  86 EKFGVELEPEVRII 99
 
Name Accession Description Interval E-value
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 7-280 4.74e-92

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: 273.43  E-value: 4.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   7 VDLRDFTTIKIGGVGSYMFFPENEKEFLDIYK--KHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIKISEtkeGIL 82
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRaaREAGLPVLVLGGGSNLLVRDdgFDGLVIRLGRLKGIEVDD---GVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  83 VKASAGVPLKDLIKLSVENNVE--EFykLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIFYTYR 159
Cdd:COG0812    78 VTAGAGENWHDLVRFALEAGLSglEF--LAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTgEVRTLSAEECGFGYR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 160 KTEFENKP--VLYGEF-LFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFS 236
Cdd:COG0812   156 DSIFKRERyiILSVTFrLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVS 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1327556126 237 QKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:COG0812   236 EKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
5-280 7.14e-77

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 235.78  E-value: 7.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   5 KNVDLRDFTTIKIGGVGSYMFFPENE---KEFLDIYKKHkNDKLCILGKGSNTIFGD--FNG-VLINTKHFYDIKISETK 78
Cdd:PRK13905   15 ENEPLARYTSFRVGGPADYLVEPADIedlQEFLKLLKEN-NIPVTVLGNGSNLLVRDggIRGvVIRLGKGLNEIEVEGNR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  79 egilVKASAGVPLKDLIKLSVENNVE--EFykLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIF 155
Cdd:PRK13905   94 ----ITAGAGAPLIKLARFAAEAGLSglEF--AAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDgEIKTLSNEELG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 156 YTYRKTEFENKP--VLYGEF-LFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKD 232
Cdd:PRK13905  168 FGYRHSALQEEGliVLSATFqLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLKGYRIGG 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1327556126 233 IGFSQKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:PRK13905  248 AQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRII 295
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 9-280 1.31e-56

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: 183.42  E-value: 1.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   9 LRDFTTIKIGGVGSYMFFPENEKEFLDIYK--KHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIKISEtkeGILVK 84
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDnaKEEDQPLLILGEGSNLLILDdgRGGVIINLGKGIDIEDDE---GEYVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  85 ASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIFYTYRKTEF 163
Cdd:TIGR00179  78 VGGGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATgKTEWLTNEQLGFGYRTSIF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 164 ENKPV---------LYGEFLFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIG 234
Cdd:TIGR00179 158 QHKYVglvlkaefqLTLGFGTRLDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAA 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1327556126 235 FSQKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:TIGR00179 238 VSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKII 283
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
5-280 9.34e-46

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 154.69  E-value: 9.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   5 KNVDLRDFTTIKIGGVGSYMFFPENEkeflDIYKKHKndklcILGKGSNTIFG-DFNGVLINTKHFYDIKIsetkEGILV 83
Cdd:PRK13904    3 KIIDFSKYSSVKIGPPLEVLVLEEID----DFSQDGQ-----IIGGANNLLISpNPKNLAILGKNFDYIKI----DGECL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  84 KASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVwyIDNDEivYKPKEEIFYTYRKTEF 163
Cdd:PRK13904   70 EIGGATKSGKIFNYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLESI--CTNGG--WIEKEDIGFGYRSSGI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 164 eNKPVLYGEFlfKKSQQDIKPLAQTINQKRmEAQPlNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFSQKHANFL 243
Cdd:PRK13904  146 -NGVILEARF--KKTHGFDEELLEAFKSMR-KNQP-KGPSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGAGFSEEHANFL 220

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1327556126 244 INYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:PRK13904  221 VNLGGATFEDALDLIELAKKRVLEEFGINLEEEVIIL 257
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
9-280 1.39e-44

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 152.86  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   9 LRDFTTIKIGGVGSYMFFPENEKEFLDI--YKKHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIkiseTKEGILVK 84
Cdd:PRK12436   25 LKNHTHIKVGGKADVFVAPTNYDEIQEVikYANKYNIPVTFLGNGSNVIIKDggIRGITVSLIHITGV----TVTGTTIV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  85 ASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEI-FDFIKGVWYIDNDEIVYKPKEEIFYTYRKTEF 163
Cdd:PRK12436  101 AQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEIsFVLTEAVVMTGDGELRTLTKEAFEFGYRKSVF 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 164 ENKP--VLYGEF-LFKKSQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFSQKHA 240
Cdd:PRK12436  181 ANNHyiILEARFeLEEGVYEEIKAKMDDLTFKRESKQPLEYPSCGSVFKRPPNNFAGKLIQESGLQGKRIGGVEVSLKHA 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1327556126 241 NFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:PRK12436  261 GFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRII 300
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
6-279 4.18e-42

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 146.13  E-value: 4.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   6 NVDLRDFTTIKIGGVGSYMFFPENEKEFLDIYK-KHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIKISETKegil 82
Cdd:PRK14653   19 NEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINlLKEGIEVKILGNGTNVLPKDepMDFVVVSTERLDDIFVDNDK---- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  83 VKASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDNDEIVYKPKEEIFYTYRKTE 162
Cdd:PRK14653   95 IICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVEVVAYDGKKIIRLGKNEIKFSYRNSI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 163 F-ENKPVLYGEFLFKKSQQD---IKPLAQTINQKRMEAQPLNMPTSGSTFKNP-KGHFAGKLLETVGLKGYRIKDIGFSQ 237
Cdd:PRK14653  175 FkEEKDLIILRVTFKLKKGNkneIYNLMLETMKKRVEKQPLEFPSAGSVFKRPrKDFYVGSAIEKLGLKGFSIGGAQISE 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1327556126 238 KHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKL 279
Cdd:PRK14653  255 KHAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEIEI 296
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 187-280 6.22e-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: 134.40  E-value: 6.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 187 QTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFSQKHANFLINYQNASFQNVIDILSIAKERVY 266
Cdd:pfam02873   6 LELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEVRERVK 85

                          90
                  ....*....|....
gi 1327556126 267 KAFNIILEEEIKLV 280
Cdd:pfam02873  86 EKFGVELEPEVRII 99
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
13-280 1.59e-36

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 131.92  E-value: 1.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  13 TTIKIGGVGSYMFFPENEKEFLDIYK--KHKNDKLCILGKGSNTIFGD--FNGVLINTKHfyDIKISETKEGILVkASAG 88
Cdd:PRK14652   28 TAVRVGGPADLLVRPADPDALSALLRavRELGVPLSILGGGANTLVADagVRGVVLRLPQ--DFPGESTDGGRLV-LGAG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  89 VPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDNDEIVYKPKEEIFYTYRKTEFENKPV 168
Cdd:PRK14652  105 APISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVTAVELATADGAGFVPAAALGYAYRTCRLPPGAV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 169 LYG-EFLFKKSqqDI---KPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFSQKHANFLI 244
Cdd:PRK14652  185 ITRvEVRLRPG--DVaasEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGHRVGGAIWSPVHANFVT 262

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1327556126 245 NYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:PRK14652  263 NLGGATARDVLALVRLARARVKERFGIALETEVRLL 298
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
9-280 1.02e-33

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 124.55  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   9 LRDFTTIKIGGVGSYMFFPENEKEFLDI--YKKHKNDKLCILGKGSNTIF--GDFNGVLINTKHFYDIKISETKegilVK 84
Cdd:PRK13906   25 LKRYTYTKTGGNADFYITPTKNEEVQAVvkYAYQNEIPVTYLGNGSNIIIreGGIRGIVISLLSLDHIEVSDDA----II 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  85 ASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIFYTYRKTEF 163
Cdd:PRK13906  101 AGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQgSLIKLTTKELELDYRNSII 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 164 ENKPVLYGEFLFKKS---QQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDIGFSQKHA 240
Cdd:PRK13906  181 QKEHLVVLEAAFTLApgkMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTKHA 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1327556126 241 NFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:PRK13906  261 GFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRII 300
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
12-280 1.04e-33

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 124.18  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  12 FTTIKIGGVGSYMFFPENEKEFLDI--YKKHKNDKLCILGKGSNTIFGD--FNGVLINTKHfYDIKISETKEGILVKASA 87
Cdd:PRK14649   12 YTSWRIGGPARYFVEPTTPDEAIAAaaWAEQRQLPLFWLGGGSNLLVRDegFDGLVARYRG-QRWELHEHGDTAEVWVEA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  88 GVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDND-EIVYKPKEEIFYTYRKTEFE-- 164
Cdd:PRK14649   91 GAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLLLNGsECVEWSVHDFAYGYRTSVLKql 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 165 -------NKP-VLYGEFLFKKSqqDIKPLAQ---TINQKRMEAQPLNmPTSGSTFKNPKGHFAGKLLETVGLKGYRIKDI 233
Cdd:PRK14649  171 radgitwRPPlVLAARFRLHRD--DPTALAArmeAIAAERKQKTPAG-SSCGSVFKNPPGDSAGRLIEAAGLKGTRIGDA 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1327556126 234 GFSQKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEIKLV 280
Cdd:PRK14649  248 EIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRII 294
PRK14650 PRK14650
UDP-N-acetylmuramate dehydrogenase;
2-277 1.53e-28

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173113 [Multi-domain]  Cd Length: 302  Bit Score: 110.70  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   2 ITNKNVDLRDFTTIKIGGVGSYMFFPENEKEFLDIYKKHKNDK--LCILGKGSNTIFGD---FNGVLINTKHFYDIKISE 76
Cdd:PRK14650   14 IKPQTKNLANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKikIFILGGGSNILINDeeeIDFPIIYTGHLNKIEIHD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  77 TKegilVKASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYID-NDEIVYKPKEEIF 155
Cdd:PRK14650   94 NQ----IVAECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKITFIDeKGKTICKKFKKEE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 156 YTYRKTEFENKP--VLYGEFLFKK-SQQDIKPLAQTINQKRMEAQPLNMPTSGSTFKNPKGHF--AGKLLETVGLKGYRI 230
Cdd:PRK14650  170 FKYKISPFQNKNtfILKATLNLKKgNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNNKAFLkpTGQIIEECKLKGLSI 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1327556126 231 KDIGFSQKHANFLINYQNASFQNVIDILSIAKERVYKAFNIILEEEI 277
Cdd:PRK14650  250 GGATVSHYHGNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEV 296
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
1-280 3.10e-28

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 110.62  E-value: 3.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   1 MITNKNVDLRDFTTIKIGGVGSYMFFPENEKEFLDIYKKHKNDKLC--ILGKGSNTIF-GDFNG-VLINtkhfyDIK--- 73
Cdd:PRK00046    1 MQLQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPvlVLGGGSNVLFtEDFDGtVLLN-----RIKgie 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  74 -ISETKEGILVKASAGVPLKDLIKLSVENNveeFY-----KLIgfPASIGGAIAMNAGAYGVEIFDFIKGVWYID--NDE 145
Cdd:PRK00046   76 vLSEDDDAWYLHVGAGENWHDLVLWTLQQG---MPglenlALI--PGTVGAAPIQNIGAYGVELKDVCDYVEALDlaTGE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 146 IVYKPKEEIFYTYR----KTEFENK---------------PVL-YGEFlfkKSQQDIKPLAQTINQK----RMEA--QPL 199
Cdd:PRK00046  151 FVRLSAAECRFGYRdsifKHEYPDRyaitavgfrlpkqwqPVLdYGDL---ARLDPDTVTAQDVFDAvcaiRRSKlpDPK 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 200 NMPTSGSTFKNP---KGHF-----------------------AGKLLETVGLKGYRIKDIGFSQKHANFLINYQNASFQn 253
Cdd:PRK00046  228 VLGNAGSFFKNPvvsAEQFeallaqypdiphypqadgsvklaAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGA- 306

                         330       340       350
                  ....*....|....*....|....*....|
gi 1327556126 254 viDILSIAK---ERVYKAFNIILEEEIKLV 280
Cdd:PRK00046  307 --DVLALARhiqQDVREKFGVELEPEPRFI 334
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
5-265 6.30e-27

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 105.67  E-value: 6.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   5 KNVDLRDFTTIKIGGvGSYMFFPENEKEFldiyKKHKNDKLCILGKGSNTIFGDfNGVLINTkhfydIKISetkeGILVK 84
Cdd:PRK14651    5 ERVPLARYTTLGVGG-PAELWTVETHEQL----AEATEAPYRVLGGGSNLLVSD-AGVPERV-----IRLG----GEFAE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  85 AS------AGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDNDEI-VYKPkEEIFYT 157
Cdd:PRK14651   70 WDldgwvgGGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVHDGGFhQYSP-DELGFG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 158 YRKTEFENKPVLygeflfKKSQQDIKPLAQTINQKRMEA-------QPlNMPTSGSTFKNPKGHFAGKLLETVGLKGYRI 230
Cdd:PRK14651  149 YRHSGLPPGHVV------TRVRLKLRPSTPEAVLAKMALvdaarkgQP-KKKSAGCAFKNPPGDSAGRLIDEAGLKGTRV 221

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1327556126 231 KDIGFSQKHANFLINYQNASFQNVIDILSIAKERV 265
Cdd:PRK14651  222 GDAMISPEHGNFIVNLGGATAADVHALLRRVRARV 256
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
2-277 1.48e-17

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 81.31  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   2 ITNKNVDLRDFTTIKIGGVGSYMFFPENEKEFLDIYKKHKNDK--LCILGKGSNTIFGD--FNGVLINTKHFYDIKISET 77
Cdd:PRK14648   11 ITRRNVPLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARipLSLIGGGSNVLIADegVPGLMLSLRRFRSLHTQTQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  78 KEG-ILVKASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYIDNDEIVYKPKEeiFY 156
Cdd:PRK14648   91 RDGsVLVHAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARTLVLHPVRSRAKE--LP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 157 TYRK-------------------TEFENKPVLYGEFLFKKS----------------------------QQDIKPLAQTI 189
Cdd:PRK14648  169 EVRKnaqdkrgeclgldggpftcSSFQTVFARAGDWGYKRSpfqsphgvelhagrrlilslcvrltpgnPAQIRKHMQEK 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 190 NQKRMEAQPLNMPTSGSTFKNPK--GHFAGKLLETVGLKGYRIKDIGFSQKHANFLINYQNASFQNVIDILSIAKERVYK 267
Cdd:PRK14648  249 IADRISKGQFRFPSAGSAFKNNPafGKPSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQRVFE 328

                         330
                  ....*....|
gi 1327556126 268 AFNIILEEEI 277
Cdd:PRK14648  329 THGVWLEREI 338
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 25-147 1.17e-14

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: 69.15  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  25 FFPENEKEFLDIYK--KHKNDKLCILGKGSNTIFGD--FNGVLINTKHFYDIkISETKEGILVKASAGVPLKDLIK-LSV 99
Cdd:pfam01565   5 VLPESEEEVAAIVRlaNENGLPVLPRGGGSSLLGGAvqTGGIVLDLSRLNGI-LEIDPEDGTATVEAGVTLGDLVRaLAA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1327556126 100 ENNVEEFYKLIGFPASIGGAIAMNAGAYGVE----IFDFIKGVWYIDND-EIV 147
Cdd:pfam01565  84 KGLLLGLDPGSGIPGTVGGAIATNAGGYGSEkyglTRDNVLGLEVVLADgEVV 136
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
6-280 3.52e-11

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 62.67  E-value: 3.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126   6 NVDLRDFTTIKIGGVGSYMFFPENEKEFLDIYKK--HKNDKLCILGKGSNTIFGD--FNG--VLINTKhfydiKISETKE 79
Cdd:PRK13903   18 DVPLAPLTTLRVGGPARRLVTCTSTEELVAAVREldAAGEPLLVLGGGSNLVIADdgFDGtvVRVATR-----GVTVDCG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126  80 GILVKASAGVPLKDLIKLSVENNVEEFYKLIGFPASIGGAIAMNAGAYGVEIFDFIKGVWYID--NDEIVYKPKEEIFYT 157
Cdd:PRK13903   93 GGLVRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTITRVRLLDrrTGEVRWVPAADLGFG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 158 YRKT-------------EFE------NKPVLYGEfLFKK---SQQDIKPLAQ---TINQKR----MEAQPLNMPT--SGS 206
Cdd:PRK13903  173 YRTSvlkhsdravvlevEFQldpsglSAPLRYGE-LARAlgvEPGERVPPAAvreAVLALRagkgMVLDPADHDTwsAGS 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327556126 207 TFKNP----------------------------KGHF---AGKLLETVGL-KGYRIKD--IGFSQKHANFLINYQNASFQ 252
Cdd:PRK13903  252 FFTNPvvspavaerlaarvaerlgdpvprypagDGGVklsAAWLIERAGFgKGYPGGGapARLSTKHTLALTNRGGATTA 331

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1327556126 253 nviDILSIAKE---RVYKAFNIILEEEIKLV 280
Cdd:PRK13903  332 ---DLVALAREvrdGVRDAFGVTLVPEPVLV 359
 
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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