|
Name |
Accession |
Description |
Interval |
E-value |
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
6-468 |
1.80e-144 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 421.01 E-value: 1.80e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 6 KKIYMVGIKGVGMTALALIYKKLANHIIGSDIgTVFPTDRILKENNIPIKGGFTPRNItDDIDLVVTTGAHGGmTNPEVE 85
Cdd:COG0773 5 MHIHFIGIGGIGMSGLAEILLALGYKVSGSDL-AESPMTERLEALGIPVFIGHDAENI-DDADLVVVSSAIPR-DNPELV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 86 EAINKGIEVLTHGQALGGLMDDfKTTISVCGAHGKTTTSALAAYVLYNSTLKGAHLVGtAEFSSLTGGDYWG-NDYFVSE 164
Cdd:COG0773 82 AARERGIPVLSRAEMLAELMRG-KRSIAVAGTHGKTTTTSMLAHILEEAGLDPTFLIG-GILNNFGTNARLGdGDYFVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 165 ADEYSNSpgtdptprFMFQHPDYIVCTNIDFDHPDRYKDLYDVQQSYKKFftTQNQDRKGILIYCGDDDVSVDASQDVPS 244
Cdd:COG0773 160 ADESDGS--------FLHYSPDIAVVTNIEADHLDIYGDLEAIKEAFHEF--ARNVPFYGLLVLCADDPGLRELLPRCGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 245 EsKYSFGFSEKCDLLLSDYGVRENKSYFTASFKGKDLGEFNLYIPGRHNVLNTGAVILLAHLLDLDIDNTRTTLSHFTGS 324
Cdd:COG0773 230 P-VITYGFSEDADYRAENIRIDGGGSTFDVLRRGEELGEVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 325 SRRFEEIFIGNDIYLYDDYAHHPKEIAAVIEAARSRFPQHRVILIFQPHTYSRTKMLAERFIEALSEADRSYVLDVFAsA 404
Cdd:COG0773 309 KRRFELKGEVGGVTVIDDYAHHPTEIAATLAAAREKYPDRRLVAVFQPHRYSRTRDFLDEFAEALSLADEVILLDIYA-A 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084038987 405 REKETQAVySSEQLIEQARLESKtNIEYLSSSNLSLL--KDVIKRGDIVITVGAGDIYKYHSELVN 468
Cdd:COG0773 388 REKPIPGV-SSEDLAEAIRKRGK-DVVYVPDLDELVEalAEIARPGDVVLTMGAGDIGGLGEKLLE 451
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
7-467 |
3.30e-118 |
|
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273433 [Multi-domain] Cd Length: 448 Bit Score: 353.92 E-value: 3.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 7 KIYMVGIKGVGMTALALIYKKLANHIIGSDIgTVFPTDRILKENNIPIKGGFTPRNItDDIDLVVTTGAHGGmTNPEVEE 86
Cdd:TIGR01082 1 KIHFVGIGGIGMSGIAEILLNRGYQVSGSDI-AENATTKRLEALGIPIYIGHSAENL-DDADVVVVSAAIKD-DNPEIVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 87 AINKGIEVLTHGQALGGLMDdFKTTISVCGAHGKTTTSALAAYVLYNSTLKGAHLVGtAEFSSLTGGDYWG-NDYFVSEA 165
Cdd:TIGR01082 78 AKERGIPVIRRAEMLAELMR-FRHSIAVAGTHGKTTTTAMIAVILKEAGLDPTVVVG-GLVKEAGTNARLGsGEYLVAEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 166 DEYSNSpgtdptprFMFQHPDYIVCTNIDFDHPDRY-KDLYDVQQSYKKFFTtqNQDRKGILIYCGDDDVSVDASQDVPS 244
Cdd:TIGR01082 156 DESDAS--------FLHLQPNVAIVTNIEPDHLDTYgSSFERLKAAFEKFIH--NLPFYGLAVICADDPVLRELVPKATE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 245 ESKYSFGFSEKCDLLLSDYGVRENKSYFTASFKGKDLGEFNLYIPGRHNVLNTGAVILLAHLLDLDIDNTRTTLSHFTGS 324
Cdd:TIGR01082 226 QVITYGGSGEDADYRAENIQQSGAEGKFSVRGKGKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 325 SRRFEEIFIGNDIYLYDDYAHHPKEIAAVIEAARSRFPQHRVILIFQPHTYSRTKMLAERFIEALSEADRSYVLDVFASA 404
Cdd:TIGR01082 306 KRRFEILGEFGGVLLIDDYAHHPTEIKATLKAARQGYPDKRIVVVFQPHRYSRTRDLFDDFAKVLSDADELILLDIYAAG 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084038987 405 REKETQAvySSEQLIEQARLESKTNIEYLSSSNLSLL--KDVIKRGDIVITVGAGDIYKYHSELV 467
Cdd:TIGR01082 386 EEPINGI--DGKSLARKITQLGKIEPYFVPDLAELVEflAAVLQSGDLILTMGAGDIIKLARELL 448
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
9-460 |
2.81e-59 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 208.52 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 9 YMVGIKGVGMTALALIYKKLANHIIGSDIGTVFPTDRIL----------KENNIPIkggftprnitddiDLVVTTGAHGG 78
Cdd:PRK14573 8 HFIGIGGIGMSALAHILLDRGYSVSGSDLSEGKTVEKLKakgarfflghQEEHVPE-------------DAVVVYSSSIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 79 MTNPEVEEAINKGIEVLTHGQALGGLMDDfKTTISVCGAHGKTTTSALAAYVLYNSTLKGAHLVGTAEFSSLTGgdYWGN 158
Cdd:PRK14573 75 KDNVEYLSAKSRGNRLVHRAELLAELMQE-QISILVSGSHGKTTVSSLITAIFQEAKKDPSYAIGGLNQEGLNG--YSGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 159 -DYFVSEADEYSNSpgtdptprFMFQHPDYIVCTNIDFDHPDRYK-DLYDVQQSYKKFFTTQNQDRKgiLIYCGDddvsv 236
Cdd:PRK14573 152 sEYFVAEADESDGS--------LKHYTPEFSVITNIDNEHLSNFEgDRELLLASIQDFARKVQQINK--CFYNGD----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 237 daSQDVPSE-SKYSFGFSEKCDLLLSDYGVRENKSYFTASFKGKDLGEFNLYIPGRHNVLNTGAVILLAHLLDLDIDNTR 315
Cdd:PRK14573 217 --CPRLKGClQGHSYGFSSSCDLHILSYYQEGWRSYFSAKFLGVVYQDIELNLVGMHNVANAAAAMGIALTLGIDEGAIR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 316 TTLSHFTGSSRRFEEIFIGNDIYLYDDYAHHPKEIAAVIEAARSRFPQHRVILIFQPHTYSRTKMLAERFIEALSEADRS 395
Cdd:PRK14573 295 NALKGFSGVQRRLERKNSSETFLFLEDYAHHPSEISCTLRAVRDAVGLRRIIAICQPHRFSRLRECLDSFPSAFQDADEV 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084038987 396 YVLDVFaSAREKETQAVySSEQLIEQARLESKTNIEYL-SSSNLSLLKDVIKRGDIVITVGAGDIY 460
Cdd:PRK14573 375 ILTDVY-SAGEEPEDSI-SYQKLAEAISQSSIVKCTYVpFHEIQRYLEQSIRVHDVCVSLGAGNIY 438
|
|
| mpl |
TIGR01081 |
UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase; Alternate name: ... |
8-398 |
1.03e-39 |
|
UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase; Alternate name: murein tripeptide ligase [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 130153 [Multi-domain] Cd Length: 448 Bit Score: 148.83 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 8 IYMVGIKGVGMTALALIYKKLANHIIGSDIGTVFPTDRILKENNIPIKGGFTPRNITDDIDLVVTTGAhggMT--NPEVE 85
Cdd:TIGR01081 2 IHILGICGTFMGGLAMIAKQLGHEVTGSDANVYPPMSTQLEAQGIEIIEGFDAAQLEPKPDLVVIGNA---MKrgNPCVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 86 EAINKGIEVLTHGQALGGLMDDFKTTISVCGAHGKTTTSALAAYVLYNSTLKGAHLVGTAEFSSLTGGDYWGNDYFVSEA 165
Cdd:TIGR01081 79 AVLNLNLPYTSGPQWLHDFVLHDRWVLAVAGTHGKTTTASMLAWVLEQCGLKPGFLIGGVPGNFGVSARLGESPFFVIEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 166 DEYsNSPGTDPTPRFMFQHPDYIVCTNIDFDHPDRYKDLYDVQQSYKKFFTTQNQDRkgiLIYCGDDDVSVDASQDVPSE 245
Cdd:TIGR01081 159 DEY-DTAFFDKRSKFVHYRPRTLVLNNLEFDHADIFDDLKAIQRQFHHLVRTVPGEG---LILCPGRDQSLKDTLAKGCW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 246 SKYSFG------FSEKcdlllsdygVRENKSYFTASFKGKDLGEFNLYIPGRHNVLNTGAVILLAHLLDLDIDNTRTTLS 319
Cdd:TIGR01081 235 SEQEFFgeqgewQAEK---------ITADGSHFDVLLDGEKVGEVKWSLVGRHNMHNALMAIAAARHVGVAIEDACEALG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 320 HFTGSSRRFEEIFIGNDIYLYDDYAHHPKEIAAVIEAARSRFPQHRVILIFQPHTYS-RTKMLAERFIEALSEADRSYVL 398
Cdd:TIGR01081 306 SFVNAKRRLELKGEANGITVYDDFAHHPTAIEATLQGLRQKVGGARILAVLEPRSNTmKLGVHKDDLAPSLGRADQVFLY 385
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
5-342 |
2.62e-24 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 104.78 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 5 GKKIYMVGIkGVGMTALALIYKKLANHIIGSDIGTVFP-TDRILKENNIPIKGGFTPRNITDDIDLVVTTGahgGM--TN 81
Cdd:COG0771 4 GKKVLVLGL-GKSGLAAARLLAKLGAEVTVSDDRPAPElAAAELEAPGVEVVLGEHPEELLDGADLVVKSP---GIppDH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 82 PEVEEAINKGIEVLT-------HGQAlgglmddfkTTISVCGAHGKTTTSALAAYVLYNSTLKgAHLVG------TAEFS 148
Cdd:COG0771 80 PLLKAARAAGIPVIGeielayrLSPA---------PIIAITGTNGKTTTTTLIGHILKAAGLR-VAVGGnigtplLDLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 149 SLTGGDYWgndyfvseADEYSnSpgtdptprfmFQ-------HPDYIVCTNIDFDHPDRYKDLydvqQSYK--KFFTTQN 219
Cdd:COG0771 150 EPEPPDVY--------VLELS-S----------FQlettpslRPDVAVILNITPDHLDRHGSM----EAYAaaKARIFAN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 220 QDRKGILIYCGDDDVSVDASQDVPSEsKYSFGFSEKcdlLLSDYGVRENKSYFTAsfKGKDLGEFN-LYIPGRHNVLNTG 298
Cdd:COG0771 207 QTPDDYAVLNADDPLTRALAEEAKAR-VVPFSLKEP---LEGGAGLEDGKLVDRA--SGEELLPVDdLRLPGRHNLENAL 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1084038987 299 AVILLAHLLDLDIDNTRTTLSHFTGSSRRFEEIFIGNDIYLYDD 342
Cdd:COG0771 281 AALAAARALGVPPEAIREALRSFKGLPHRLEFVAEINGVRFIND 324
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
191-370 |
3.95e-20 |
|
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 92.45 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 191 TNIDFDHPDRYKDLydvqQSY----KKFFTTQNQDRKGILiyCGDDDVSVDASQDVPSeSKYSFGFSEKCDLLLSDYGVR 266
Cdd:COG0769 176 TNLTRDHLDYHGTM----EAYfaakARLFDQLGPGGAAVI--NADDPYGRRLAAAAPA-RVITYGLKADADLRATDIELS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 267 ENKSYFTASFKGKDlGEFNLYIPGRHNVLNTGAVILLAHLLDLDIDNTRTTLSHFTGSSRRFEEIFIGNDIYLYDDYAHH 346
Cdd:COG0769 249 ADGTRFTLVTPGGE-VEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVDGGQGPTVIVDYAHT 327
|
170 180
....*....|....*....|....
gi 1084038987 347 PKEIAAVIEAARsRFPQHRVILIF 370
Cdd:COG0769 328 PDALENVLEALR-PHTKGRLIVVF 350
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
224-342 |
3.73e-17 |
|
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 83.61 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 224 GILIYCGDDDVsVDASQDVPSESKYSFGFSEKCDLLLSDYGVRENKSYFTASFKGKDLgEFNLYIPGRHNVLNTGAVILL 303
Cdd:COG0770 213 GVAVLNADDPL-LAALAERAKARVLTFGLSEDADVRAEDIELDEDGTRFTLHTPGGEL-EVTLPLPGRHNVSNALAAAAV 290
|
90 100 110
....*....|....*....|....*....|....*....
gi 1084038987 304 AHLLDLDIDNTRTTLSHFTGSSRRFEEIFIGNDIYLYDD 342
Cdd:COG0770 291 ALALGLDLEEIAAGLAAFQPVKGRLEVIEGAGGVTLIDD 329
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
80-342 |
4.97e-17 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 83.16 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 80 TNPEVEEAINKGIEVLTHGQALGGLMDdfKTTISVCGAHGKTTTSALAAYVLYNSTLKgAHLVGTAEFSSLTGGDYWGND 159
Cdd:TIGR01087 75 DHPLVQAAAKRGIPVVGDIELFLRLVP--LPVVAITGTNGKTTTTSLLYHLLKAAGLK-AFLGGNIGTPALEVLDQEGAE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 160 YFVSEADEYS--NSPGTDPtprfmfqhPDYIVcTNIDFDHPDRYKDLYDVQQSYKKFFTTQNQDRKGILIycgdDDVSVD 237
Cdd:TIGR01087 152 LYVLELSSFQleTTESLRP--------EIALI-LNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLN----ADDPRF 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 238 ASQDVPSESKYSFGFSEKcdLLLSDYGVRENKSYFtasfKGKDLgefNLYIPGRHNVLNTGAVILLAHLLDLDIDNTRTT 317
Cdd:TIGR01087 219 ARLAQKSKAQVIWFSVEK--DAERGLCIRDGGLYL----KPNDL---EGSLLGLHNAENILAAIALAKSLGLNLEAILEA 289
|
250 260
....*....|....*....|....*
gi 1084038987 318 LSHFTGSSRRFEEIFIGNDIYLYDD 342
Cdd:TIGR01087 290 LRSFKGLPHRLEYVGQKNGVHFYND 314
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
1-329 |
3.66e-16 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 80.40 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 1 MITTGKKIYMVGIkGVGMTALALIYKKLANHIIGSDIGT-VFPTDRI--LKENNIPIKGGFTPRNITDDIDLVVTT-GAh 76
Cdd:PRK14106 1 MELKGKKVLVVGA-GVSGLALAKFLKKLGAKVILTDEKEeDQLKEALeeLGELGIELVLGEYPEEFLEGVDLVVVSpGV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 77 gGMTNPEVEEAINKGIEVLthGQALGGLMDDFKTTISVCGAHGKTTTSALAAYVLYNSTLK-------GAHLVGTAEfss 149
Cdd:PRK14106 79 -PLDSPPVVQAHKKGIEVI--GEVELAYRFSKAPIVAITGTNGKTTTTTLLGEIFKNAGRKtlvagniGYPLIDAVE--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 150 ltggDYWGNDYFVSEAdeysNSPGTDPTPRFmfqHPDYIVCTNIDFDHPDRYKDLYDVQQSYKKFFttQNQDRKGILIYC 229
Cdd:PRK14106 153 ----EYGEDDIIVAEV----SSFQLETIKEF---KPKVGCILNITPDHLDRHKTMENYIKAKARIF--ENQRPSDYTVLN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 230 GDDDVSVDASQDVPSESKYsfgFSEKcDLLLSDYGVRENKSYftASFKGK-----DLGEfnLYIPGRHNVLNTGAVILLA 304
Cdd:PRK14106 220 YDDPRTRSLAKKAKARVIF---FSRK-SLLEEGVFVKNGKIV--ISLGGKeeeviDIDE--IFIPGEHNLENALAATAAA 291
|
330 340
....*....|....*....|....*
gi 1084038987 305 HLLDLDIDNTRTTLSHFTGSSRRFE 329
Cdd:PRK14106 292 YLLGISPDVIANTLKTFKGVEHRIE 316
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
99-370 |
5.21e-16 |
|
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273435 [Multi-domain] Cd Length: 464 Bit Score: 80.05 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 99 QALGGLMDDF-------KTTISVCGAHGKTTTSALAAYVLYNSTLKGAhLVGTAEF-----------SSLTGGDYW---- 156
Cdd:TIGR01085 68 HALSSLAAAFyghpskkLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTG-LIGTIGYrlggndliknpAALTTPEALtlqs 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 157 --------GNDYFVSEAdeysNSPGTDpTPRFMFQHPDYIVCTNIDFDHPDRYKDLYDVQQSYKKFFTTQNQDRKGILiy 228
Cdd:TIGR01085 147 tlaemveaGAQYAVMEV----SSHALA-QGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTELGLKRFAVI-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 229 CGDDDVSVD----ASQDVPSESKYSFGFSEKCDLLLSDYGVRENKSYFTASFKGkdlGEFNLYIP--GRHNVLNTGAVIL 302
Cdd:TIGR01085 220 NLDDEYGAQfvkrLPKDITVSAITQPADGRAQDIKITDSGYSFEGQQFTFETPA---GEGHLHTPliGRFNVYNLLAALA 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084038987 303 LAH-LLDLDIDNTRTTLSHFTGSSRRFEEIFIGNDIYLYDDYAHHPKEIAAVIEAARsRFPQHRVILIF 370
Cdd:TIGR01085 297 TLLhLGGIDLEDIVAALEKFRGVPGRMELVDGGQKFLVIVDYAHTPDALEKALRTLR-KHKDGRLIVVF 364
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
114-304 |
1.35e-12 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 66.56 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 114 VCGAHGKTTTSALAAYVLynstLKGAHLVGTAEF----SSLTGGDYWGN------------DYFVSEADeySNSPGTDPT 177
Cdd:pfam08245 1 VTGTNGKTTTTELIAAIL----SLAGGVIGTIGTyigkSGNTTNNAIGLpltlaemveagaEYAVLEVS--SHGLGEGRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 178 pRFMFQhPDYIVCTNIDFDHPDRYKDLYDVQQSYKKFFTTQNQDrkGILIYCGDDDVSVDASQD--VPSESKYSFGFSEK 255
Cdd:pfam08245 75 -SGLLK-PDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPED--GIAVINADDPYGAFLIAKlkKAGVRVITYGIEGE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084038987 256 CDLLLSDYGVRENKSYFTASFKGKDLGEFNLYIPGRHNVLNTGAVILLA 304
Cdd:pfam08245 151 ADLRAANIELSSDGTSFDLFTVPGGELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
263-370 |
5.23e-12 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 67.46 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 263 YGVRENKSYFTA-----SFKGKDL---GEFNLYIPGRHNVLNTGAVILLAHLLDLDIDNTRTTLSHFTGSSRRFEEIFIG 334
Cdd:PRK00139 241 YAVSMAGADLRAtdveyTDSGQTFtlvTEVESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRMERVDAG 320
|
90 100 110
....*....|....*....|....*....|....*.
gi 1084038987 335 NDIYLYDDYAHHPKEIAAVIEAARsRFPQHRVILIF 370
Cdd:PRK00139 321 QGPLVIVDYAHTPDALEKVLEALR-PHAKGRLICVF 355
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
326-408 |
2.23e-11 |
|
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 59.67 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 326 RRFEEIFIGNDIYLYDDYAHHPKEIAAVIEAARSRFPQhRVILIFQP--HtysRTKMLAERFIEALSE-ADRSYVLDVFA 402
Cdd:pfam02875 3 GRLEVVGENNGVLVIDDYAHNPDAMEAALRALRNLFPG-RLILVFGGmgD---RDAEFHALLGRLAAAlADVVILTGDYP 78
|
....*.
gi 1084038987 403 SAREKE 408
Cdd:pfam02875 79 RAEDPG 84
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
185-356 |
2.75e-07 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273468 [Multi-domain] Cd Length: 417 Bit Score: 52.65 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 185 PDYIVCTNIDFDHPDRYKDLYDVQQSYKKFFttQNQDRKGILIYCGDDDVSVDASQDVPSESKYSFGFsekcdlllsdyg 264
Cdd:TIGR01143 150 PDIAVITNIGPAHLEGFGSLEGIAEAKGEIL--QGLKENGIAVINADDPAFADLAKRLPNRNILSFGF------------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 265 vrENKSYFTASFKGKDLG-----------EFNLYIP--GRHNVLNTGAVILLAHLLDLDIDNTRTTLSHFTGSSRRFeEI 331
Cdd:TIGR01143 216 --EGGDFVAKDISYSALGstsftlvapggEFEVSLPllGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRF-EV 292
|
170 180
....*....|....*....|....*.
gi 1084038987 332 FIGNDIYLYDD-YAHHPKEIAAVIEA 356
Cdd:TIGR01143 293 QTKNGLTLIDDtYNANPDSMRAALDA 318
|
|
| Mur_ligase |
pfam01225 |
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes ... |
7-109 |
3.98e-06 |
|
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460121 [Multi-domain] Cd Length: 84 Bit Score: 44.92 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 7 KIYMVGIKGVGMTALALIYKKLANHIIGSDIgtvfptDRILKENNIPIKGGFTPRNITDDidlvvttgahggmTNPEVEE 86
Cdd:pfam01225 1 EIHFVGIDGRGMSPGALFLALKGYRVDGSDF------IESLIALGAAAVVGHDAANNISP-------------DNPELEA 61
|
90 100
....*....|....*....|...
gi 1084038987 87 AINKGIEVLTHGQALGGLMDDFK 109
Cdd:pfam01225 62 AKVPGIPVIDRREALAELAAAFY 84
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
67-369 |
9.67e-05 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 45.08 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 67 IDLVVTTGAHGGMTNPEVEEAINKGIEVLTHGQALG----GLMDDFKT-TISVCGAHGKTTTSALAAYVLYNSTLKGAHL 141
Cdd:PRK11929 556 LPQAFAAGACAAVVERQVADVDLPQIVVDDTRAALGrlatAWRARFSLpVVAITGSNGKTTTKEMIAAILAAWQGEDRVL 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 142 VGTAEFSSLTG---------GDYwgnDYFVSEADeySNSPGTDPTPRFMFQhPDYIVCTNIDFDHPDRYKDLYDVQQSYK 212
Cdd:PRK11929 636 ATEGNFNNEIGvpltllrlrAQH---RAAVFELG--MNHPGEIAYLAAIAA-PTVALVTNAQREHQEFMHSVEAVARAKG 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 213 KFFTTQNQDrkGILIYCGDDDVSVDASQDVPSESKYSFGFSEKCDLLL----SDYGVRENKSYFTASFKGKDLGEFNLYI 288
Cdd:PRK11929 710 EIIAALPED--GVAVVNGDDPYTAIWAKLAGARRVLRFGLQPGADVYAekiaKDISVGEAGGTRCQVVTPAGSAEVYLPL 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084038987 289 PGRHNVLNTGAVILLAHLLDLDIDNTRTTLSHFTGSSRRFEEIFIGNDIYLYDD-YAHHPKEIAAVIEAArSRFPQHRVI 367
Cdd:PRK11929 788 IGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCGTRIIDDtYNANPDSMRAAIDVL-AELPNGPRA 866
|
..
gi 1084038987 368 LI 369
Cdd:PRK11929 867 LV 868
|
|
| PRK14093 |
PRK14093 |
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ... |
249-321 |
5.27e-04 |
|
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional
Pssm-ID: 184501 [Multi-domain] Cd Length: 479 Bit Score: 42.45 E-value: 5.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084038987 249 SFGFSEKCDLLLSDYGVRENKSYFTASFKGKDLgEFNLYIPGRHNVLNTGAVILLAHLLDLDIDNTRTTLSHF 321
Cdd:PRK14093 249 SFGADEKADARLLDVALHADCSAVHADILGHDV-TYKLGMPGRHIAMNSLAVLAAAELAGADLALAALALSQV 320
|
|
| |
