|
Name |
Accession |
Description |
Interval |
E-value |
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
12-395 |
7.19e-141 |
|
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: 409.08 E-value: 7.19e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 12 AQAFIASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTSRFDTGFhtTTPSPWQIQKYLR 91
Cdd:COG0769 64 ALALLAAAFYGHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSL--TTPEALDLQRLLA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 92 KAVNLGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFR---KVNFSILNFDDQSFDFL 168
Cdd:COG0769 142 EMVDAGVTHVVMEVSSHALDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDqlgPGGAAVINADDPYGRRL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 169 KSNVDGKIITYSAKSQADFNPKRL------------------PLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNN 230
Cdd:COG0769 222 AAAAPARVITYGLKADADLRATDIelsadgtrftlvtpggevEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 231 FGGVPGRMNEVDLGQNFQVFIDFAHTPNALKEALKTLKSQIPNpksKLITVFGSAGERDKAKRPLMGKIAAGIADVSILT 310
Cdd:COG0769 302 LKGVPGRMERVDGGQGPTVIVDYAHTPDALENVLEALRPHTKG---RLIVVFGCGGDRDRGKRPLMGEIAARLADVVIVT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 311 AEDPRREKVEDICKSIAEGFSEGKKegkdYHIIYDRAKAITFAVNLAADGDIVSLFGKAHEKSMCFGKKEYPWDEFVAVE 390
Cdd:COG0769 379 SDNPRSEDPAAIIADILAGIPGAGK----VLVIPDRAEAIRYAIALAKPGDVVLIAGKGHETYQIIGGVKIPFDDREVAR 454
|
....*
gi 818551063 391 KAINE 395
Cdd:COG0769 455 EALAE 459
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
14-396 |
3.62e-121 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 359.06 E-value: 3.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 14 AFIASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTSRFDTGFhtTTPSPWQIQKYLRKA 93
Cdd:PRK00139 81 ALLAAAFYGHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELIPSGL--TTPDALDLQRLLAEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 94 VNLGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKV-NFSILNFDDQSFDFLKSNV 172
Cdd:PRK00139 159 VDAGVTYAAMEVSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLFSELgLAAVINADDEVGRRLLALP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 173 DgkiiTYSAK-SQADFNPKRL-------------PLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRM 238
Cdd:PRK00139 239 D----AYAVSmAGADLRATDVeytdsgqtftlvtEVESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 239 NEVDLGQNFQVFIDFAHTPNALKEALKTLKsqiPNPKSKLITVFGSAGERDKAKRPLMGKIAAGIADVSILTAEDPRREK 318
Cdd:PRK00139 315 ERVDAGQGPLVIVDYAHTPDALEKVLEALR---PHAKGRLICVFGCGGDRDKGKRPLMGAIAERLADVVIVTSDNPRSED 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818551063 319 VEDICKSIAEGFsegkkegkdYHIIYDRAKAITFAVNLAADGDIVSLFGKAHEKSMCFGKKEYPWDEFVAVEKAINER 396
Cdd:PRK00139 392 PAAIIADILAGI---------YDVIEDRAEAIRYAIAQAKPGDVVLIAGKGHEDYQIIGGVKIPFDDREVAREALAER 460
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
17-385 |
6.00e-116 |
|
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: 345.84 E-value: 6.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 17 ASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLG-ALVGTSRFDTGFHTTTPSPWQIQKYLRKAVN 95
Cdd:TIGR01085 74 AAAFYGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGyRLGGNDLIKNPAALTTPEALTLQSTLAEMVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 96 LGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKV---NFSILNFDD---------- 162
Cdd:TIGR01085 154 AGAQYAVMEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTELglkRFAVINLDDeygaqfvkrl 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 163 ----------QSFDFLKSNVDGKIITYSAKSQA---DFNPKRLPLRLKIPGDYNLRNALAAAAAVSSL-RIKKKKILSVL 228
Cdd:TIGR01085 234 pkditvsaitQPADGRAQDIKITDSGYSFEGQQftfETPAGEGHLHTPLIGRFNVYNLLAALATLLHLgGIDLEDIVAAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 229 NNFGGVPGRMNEVDLGQNFQVFIDFAHTPNALKEALKTLKsqiPNPKSKLITVFGSAGERDKAKRPLMGKIAAGIADVSI 308
Cdd:TIGR01085 314 EKFRGVPGRMELVDGGQKFLVIVDYAHTPDALEKALRTLR---KHKDGRLIVVFGCGGDRDRGKRPLMGAIAEQLADLVI 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818551063 309 LTAEDPRREKVEDICKSIAEGFSEGKKegkdYHIIYDRAKAITFAVNLAADGDIVSLFGKAHEKSMCFGKKEYPWDE 385
Cdd:TIGR01085 391 LTSDNPRGEDPEQIIADILAGISEKEK----VVIIADRRQAIRYAISNAKAGDVVLIAGKGHEDYQIIGGETIPFDD 463
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
33-206 |
3.06e-46 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 157.47 E-value: 3.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 33 ITGTDGKTTTVWMVYEILKNSGFKVsqisslgALVGTSRFDTGFhtTTPSPWQIQKYLRKAVNLGNKYFVLEATSHGLDQ 112
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGVI-------GTIGTYIGKSGN--TTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 113 NRLAF-VKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKV---NFSILNFDDQSFDFLK---SNVDGKIITYSAKSQA 185
Cdd:pfam08245 72 GRLSGlLKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLpedGIAVINADDPYGAFLIaklKKAGVRVITYGIEGEA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818551063 186 DFNP-------------------KRLPLRLKIPGDYNLRN 206
Cdd:pfam08245 152 DLRAanielssdgtsfdlftvpgGELEIEIPLLGRHNVYN 191
|
|
| F430_CfbE |
NF033197 |
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ... |
30-274 |
2.03e-07 |
|
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.
Pssm-ID: 467992 [Multi-domain] Cd Length: 419 Bit Score: 52.71 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 30 VIGITGTDGKTTTVWMVYEILKNSGfkVSQISSLGALVGTSRFDTGFHTTTPSpwQIQKYLRKAVNLGNK---YFVLEaT 106
Cdd:NF033197 94 FIEITGVKGKTTTAELLAHILSDEY--VLLHTSRGTERYPEGELSNKGSITPA--SILNALELAEEIGIDdygFLIFE-V 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 107 SHGLdqnrlaFVKFKIAVITNVTHehlDYH--KSQKRYLGAKAKLF--RKVNFSILNFDdqsfDFLKSNVDGKIITYSAK 182
Cdd:NF033197 169 SLGG------TGAGDVGIITNILE---DYPiaGGKRSASAAKLQSLknAKVGSINVADL----GIYINGKNKLVITVAGV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 183 SQADFNPKR-----LPLRLK--IPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRMNEVDLGQNfqVFIDFAh 255
Cdd:NF033197 236 EILSKYPLRfkygnTEFEFNplLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAVKKEGGV--VIVDNI- 312
|
250 260
....*....|....*....|....*
gi 818551063 256 tpN------ALKEALKTLKSQIPNP 274
Cdd:NF033197 313 --NpglnvkAIEYALDDALELLGDG 335
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
12-395 |
7.19e-141 |
|
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: 409.08 E-value: 7.19e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 12 AQAFIASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTSRFDTGFhtTTPSPWQIQKYLR 91
Cdd:COG0769 64 ALALLAAAFYGHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSL--TTPEALDLQRLLA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 92 KAVNLGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFR---KVNFSILNFDDQSFDFL 168
Cdd:COG0769 142 EMVDAGVTHVVMEVSSHALDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDqlgPGGAAVINADDPYGRRL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 169 KSNVDGKIITYSAKSQADFNPKRL------------------PLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNN 230
Cdd:COG0769 222 AAAAPARVITYGLKADADLRATDIelsadgtrftlvtpggevEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 231 FGGVPGRMNEVDLGQNFQVFIDFAHTPNALKEALKTLKSQIPNpksKLITVFGSAGERDKAKRPLMGKIAAGIADVSILT 310
Cdd:COG0769 302 LKGVPGRMERVDGGQGPTVIVDYAHTPDALENVLEALRPHTKG---RLIVVFGCGGDRDRGKRPLMGEIAARLADVVIVT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 311 AEDPRREKVEDICKSIAEGFSEGKKegkdYHIIYDRAKAITFAVNLAADGDIVSLFGKAHEKSMCFGKKEYPWDEFVAVE 390
Cdd:COG0769 379 SDNPRSEDPAAIIADILAGIPGAGK----VLVIPDRAEAIRYAIALAKPGDVVLIAGKGHETYQIIGGVKIPFDDREVAR 454
|
....*
gi 818551063 391 KAINE 395
Cdd:COG0769 455 EALAE 459
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
14-396 |
3.62e-121 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 359.06 E-value: 3.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 14 AFIASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTSRFDTGFhtTTPSPWQIQKYLRKA 93
Cdd:PRK00139 81 ALLAAAFYGHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELIPSGL--TTPDALDLQRLLAEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 94 VNLGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKV-NFSILNFDDQSFDFLKSNV 172
Cdd:PRK00139 159 VDAGVTYAAMEVSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLFSELgLAAVINADDEVGRRLLALP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 173 DgkiiTYSAK-SQADFNPKRL-------------PLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRM 238
Cdd:PRK00139 239 D----AYAVSmAGADLRATDVeytdsgqtftlvtEVESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 239 NEVDLGQNFQVFIDFAHTPNALKEALKTLKsqiPNPKSKLITVFGSAGERDKAKRPLMGKIAAGIADVSILTAEDPRREK 318
Cdd:PRK00139 315 ERVDAGQGPLVIVDYAHTPDALEKVLEALR---PHAKGRLICVFGCGGDRDKGKRPLMGAIAERLADVVIVTSDNPRSED 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818551063 319 VEDICKSIAEGFsegkkegkdYHIIYDRAKAITFAVNLAADGDIVSLFGKAHEKSMCFGKKEYPWDEFVAVEKAINER 396
Cdd:PRK00139 392 PAAIIADILAGI---------YDVIEDRAEAIRYAIAQAKPGDVVLIAGKGHEDYQIIGGVKIPFDDREVAREALAER 460
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
17-385 |
6.00e-116 |
|
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: 345.84 E-value: 6.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 17 ASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLG-ALVGTSRFDTGFHTTTPSPWQIQKYLRKAVN 95
Cdd:TIGR01085 74 AAAFYGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGyRLGGNDLIKNPAALTTPEALTLQSTLAEMVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 96 LGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKV---NFSILNFDD---------- 162
Cdd:TIGR01085 154 AGAQYAVMEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTELglkRFAVINLDDeygaqfvkrl 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 163 ----------QSFDFLKSNVDGKIITYSAKSQA---DFNPKRLPLRLKIPGDYNLRNALAAAAAVSSL-RIKKKKILSVL 228
Cdd:TIGR01085 234 pkditvsaitQPADGRAQDIKITDSGYSFEGQQftfETPAGEGHLHTPLIGRFNVYNLLAALATLLHLgGIDLEDIVAAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 229 NNFGGVPGRMNEVDLGQNFQVFIDFAHTPNALKEALKTLKsqiPNPKSKLITVFGSAGERDKAKRPLMGKIAAGIADVSI 308
Cdd:TIGR01085 314 EKFRGVPGRMELVDGGQKFLVIVDYAHTPDALEKALRTLR---KHKDGRLIVVFGCGGDRDRGKRPLMGAIAEQLADLVI 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818551063 309 LTAEDPRREKVEDICKSIAEGFSEGKKegkdYHIIYDRAKAITFAVNLAADGDIVSLFGKAHEKSMCFGKKEYPWDE 385
Cdd:TIGR01085 391 LTSDNPRGEDPEQIIADILAGISEKEK----VVIIADRRQAIRYAISNAKAGDVVLIAGKGHEDYQIIGGETIPFDD 463
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
16-398 |
9.77e-83 |
|
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: 271.96 E-value: 9.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 16 IASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTSRFDTGFhtTTPSPWQIQKYLRKAVN 95
Cdd:PRK11929 100 LAARWYGRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGARLDGRLIPGSL--TTPDAIILHRILARMRA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 96 LGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKV---NFSILNFDD---------- 162
Cdd:PRK11929 178 AGADAVAMEASSHGLEQGRLDGLRIAVAGFTNLTRDHLDYHGTMQDYEEAKAALFSKLpglGAAVINADDpaaarllaal 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 163 ---QSFDFLKSNVDGKIitYSAKSQAD---------FNPKRLPLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNN 230
Cdd:PRK11929 258 prgLKVGYSPQNAGADV--QARDLRATahgqvftlaTPDGSYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 231 FGGVPGRMNEVD---LGQNFQVFIDFAHTPNALKEALKTLKSQIPNPKSKLITVFGSAGERDKAKRPLMGKIAAGIADVS 307
Cdd:PRK11929 336 VSPVPGRMERVGptaGAQGPLVVVDYAHTPDALAKALTALRPVAQARNGRLVCVFGCGGDRDKGKRPEMGRIAAELADRV 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 308 ILTAEDPRREKVEDICKSIAEGFSEGKKegkdYHIIYDRAKAITFAVNLAADGDIVSLFGKAHEKSMCFGKKEYPWDEFV 387
Cdd:PRK11929 416 VVTSDNPRSEAPEAIIDQILAGIPAGAR----VFVISDRAEAIRQAIWMAAPGDVILIAGKGHETYQEIGGRKLFFDDRE 491
|
410
....*....|.
gi 818551063 388 AVEKAINERLK 398
Cdd:PRK11929 492 WARRALLARIS 502
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
12-394 |
7.59e-52 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 180.23 E-value: 7.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 12 AQAFIASVYFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGfKVSQISSL-GALVGTSRFDTgfHTTTPSPWQIQKYL 90
Cdd:PRK14022 94 AMSLIAMEFYDNPQHKLKLLAFTGTKGKTTAAYFAYHILKQLH-KPAMLSTMnTTLDGETFFKS--ALTTPESLDLFKMM 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 91 RKAVNLGNKYFVLEATSHGLDQNRLAFVKFKIAVITNVTHEHLDY--HKSQKRYLGAKAKLFRKVNFSILNFDDQSFDFL 168
Cdd:PRK14022 171 AEAVDNGMTHLIMEVSSQAYLVGRVYGLTFDVGVFLNITPDHIGPieHPTFEDYFYHKRLLMENSKAVVVNSDMDHFSEL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 169 KSNV-DGKIITYSAKSQADFNPKR---LPLRLKIPGDY--------NLRNALAAAAAVSSLRIKKKKILSVLNNfGGVPG 236
Cdd:PRK14022 251 LEQVtPQEHDFYGIDSENQIMASNafsFEATGKLAGTYdiqligkfNQENAMAAGLACLRLGASLEDIQKGIAQ-TPVPG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 237 RMNEVDLGQNFQVFIDFAHTPNALKEALKTLKsqiPNPKSKLITVFGSAGERDKAKRPLMGKIAAGIADVS-ILTAEDPR 315
Cdd:PRK14022 330 RMEVLTQSNGAKVFIDYAHNGDSLNKLIDVVE---EHQKGKLILLLGAAGNKGESRRPDFGRVANRHPYLQvILTADDPN 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 316 REKVEDICKSIAEGFSegkkegKDYHIIYDRAKAITFAVNLA-ADGDIVSLFGKAHEksmCF----GKKE-YPWDEFVAv 389
Cdd:PRK14022 407 NEDPKMITQEIASHIT------HPVEIIDDRAEAIKHAMSITeGPGDAVIIAGKGAD---AYqivpGHRDdYIGDEAAA- 476
|
....*
gi 818551063 390 EKAIN 394
Cdd:PRK14022 477 KKYLG 481
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
33-206 |
3.06e-46 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 157.47 E-value: 3.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 33 ITGTDGKTTTVWMVYEILKNSGFKVsqisslgALVGTSRFDTGFhtTTPSPWQIQKYLRKAVNLGNKYFVLEATSHGLDQ 112
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGVI-------GTIGTYIGKSGN--TTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 113 NRLAF-VKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKV---NFSILNFDDQSFDFLK---SNVDGKIITYSAKSQA 185
Cdd:pfam08245 72 GRLSGlLKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLpedGIAVINADDPYGAFLIaklKKAGVRVITYGIEGEA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 818551063 186 DFNP-------------------KRLPLRLKIPGDYNLRN 206
Cdd:pfam08245 152 DLRAanielssdgtsfdlftvpgGELEIEIPLLGRHNVYN 191
|
|
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
25-363 |
8.94e-31 |
|
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: 122.48 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 25 SRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSqisslgALVG--TSRFDTGFHtttpspwqiqkylrkavnLG-NKYF 101
Cdd:COG0773 101 MRGKRSIAVAGTHGKTTTTSMLAHILEEAGLDPT------FLIGgiLNNFGTNAR------------------LGdGDYF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 102 VLEAtshglDQNRLAFVKFK--IAVITNVTHEHLDYHKSQKRYLGAKAKLFRKVNFS---ILNFDDQSFDFLKSNVDGKI 176
Cdd:COG0773 157 VAEA-----DESDGSFLHYSpdIAVVTNIEADHLDIYGDLEAIKEAFHEFARNVPFYgllVLCADDPGLRELLPRCGRPV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 177 ITYSAKSQADF-------------------NPKRLPLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGR 237
Cdd:COG0773 232 ITYGFSEDADYraeniridgggstfdvlrrGEELGEVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGVKRR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 238 MNEVDLGQNFQVFIDFAHTPNALKEALKTLKSQIPNpkSKLITVFgsagE-----RDKAkrpLMGKIAA--GIADVSILT 310
Cdd:COG0773 312 FELKGEVGGVTVIDDYAHHPTEIAATLAAAREKYPD--RRLVAVF----QphrysRTRD---FLDEFAEalSLADEVILL 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 818551063 311 AEDPRREK------VEDICKSIaegfsegKKEGKDYHIIYDRAKAITFAVNLAADGDIV 363
Cdd:COG0773 383 DIYAAREKpipgvsSEDLAEAI-------RKRGKDVVYVPDLDELVEALAEIARPGDVV 434
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
30-365 |
2.49e-28 |
|
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: 115.18 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 30 VIGITGTDGKTTTVWMVYEILKNSGFKVsqisslgALVGtsrfdtgfhtttpspwqiqkylrkavNLG------------ 97
Cdd:COG0771 107 IIAITGTNGKTTTTTLIGHILKAAGLRV-------AVGG--------------------------NIGtplldlllepep 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 98 NKYFVLEATSHGLDqnRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFR---KVNFSILNFDDQSFDFLKSNVDG 174
Cdd:COG0771 154 PDVYVLELSSFQLE--TTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFAnqtPDDYAVLNADDPLTRALAEEAKA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 175 KIITYSAKSQAD-----------FNPKRLPL----RLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRM- 238
Cdd:COG0771 232 RVVPFSLKEPLEggagledgklvDRASGEELlpvdDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLe 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 239 -----NEVDlgqnfqvFID--FAHTPNALKEALKTLKSQIpnpksKLItvfgsAGERDKA--KRPLMGKIAAGIADVsIL 309
Cdd:COG0771 312 fvaeiNGVR-------FINdsKATNPDATLAALESFDGPV-----VLI-----AGGLDKGadFSPLAPAVAERVKAV-VL 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 818551063 310 TAEDprREKvedicksIAEGFsegKKEGKDYHIIYDRAKAITFAVNLAADGDIVSL 365
Cdd:COG0771 374 IGED--AEK-------IAAAL---AGAGVPVVIVETMEEAVAAAAELARPGDVVLL 417
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
28-365 |
1.83e-26 |
|
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: 110.12 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 28 LTVIGITGTDGKTTTVWMVYEILKNSGFKVsqisSLGALVGTSRFDTGFHTttpspwqiqkylrkavnlGNKYFVLEATS 107
Cdd:TIGR01087 102 LPVVAITGTNGKTTTTSLLYHLLKAAGLKA----FLGGNIGTPALEVLDQE------------------GAELYVLELSS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 108 HGL-DQNRLafvKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLF---RKVNFSILNFDDQSFDFLKSNVDGKIITYSAKS 183
Cdd:TIGR01087 160 FQLeTTESL---RPEIALILNISEDHLDWHGSFEDYVAAKLKIFarqTEGDVAVLNADDPRFARLAQKSKAQVIWFSVEK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 184 QAD-----------FNPKRLPLRLkiPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRMNEVDLGQNFQvFID 252
Cdd:TIGR01087 237 DAErglcirdgglyLKPNDLEGSL--LGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVH-FYN 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 253 --FAHTPNALKEALKTLKSQIpnpksKLItvfgsAGERDK-----AKRPLMGKIAAGIadvsILTAEDprREKVEDICKS 325
Cdd:TIGR01087 314 dsKATNVHATLAALSAFDNPV-----ILI-----VGGDDKgadfsPLAPAAAGKVKAV----LAIGED--AAKIAPLLKE 377
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 818551063 326 IAEgfsegkkegkDYHIIYDRAKAITFAVNLAADGDIVSL 365
Cdd:TIGR01087 378 AGL----------SVYLVESLEEAVQAAREVASPGDVVLL 407
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
25-363 |
2.93e-22 |
|
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: 98.15 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 25 SRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQIssLGALVGtsRFDTGfhtttpspwqiqkylrkAVNLGNKYFVLE 104
Cdd:TIGR01082 96 MRFRHSIAVAGTHGKTTTTAMIAVILKEAGLDPTVV--VGGLVK--EAGTN-----------------ARLGSGEYLVAE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 105 AtshglDQNRLAFVKFK--IAVITNVTHEHLD-YHKSQKRYLGAKAKLFRKVNF---SILNFDDQSFDFLKSNVDGKIIT 178
Cdd:TIGR01082 155 A-----DESDASFLHLQpnVAIVTNIEPDHLDtYGSSFERLKAAFEKFIHNLPFyglAVICADDPVLRELVPKATEQVIT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 179 Y-SAKSQADF-------------------NPKRLPLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRM 238
Cdd:TIGR01082 230 YgGSGEDADYraeniqqsgaegkfsvrgkGKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGVKRRF 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 239 NEvdLGQ-NFQVFI-DFAHTPNALKEALKTLKSQIPNpkSKLITVFGSagERDKAKRPLMGKIAAGIADVSILTAED--- 313
Cdd:TIGR01082 310 EI--LGEfGGVLLIdDYAHHPTEIKATLKAARQGYPD--KRIVVVFQP--HRYSRTRDLFDDFAKVLSDADELILLDiya 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 818551063 314 PRREKVEDI-CKSIAegFSEGKKEGKDYHIIYDRAKAITFAVNLAADGDIV 363
Cdd:TIGR01082 384 AGEEPINGIdGKSLA--RKITQLGKIEPYFVPDLAELVEFLAAVLQSGDLI 432
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
30-242 |
2.90e-21 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 95.04 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 30 VIGITGTDGKTTTVWMVYEILKNSGFKVsqisslgaLVGTsrfDTGFhtttPSPWQIQKYLRKAVnlgnkyFVLEATSHG 109
Cdd:PRK14106 110 IVAITGTNGKTTTTTLLGEIFKNAGRKT--------LVAG---NIGY----PLIDAVEEYGEDDI------IVAEVSSFQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 110 LDQNRlaFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLF---RKVNFSILNFDDQSFDFLKSNVDGKIITYSAKSQ-- 184
Cdd:PRK14106 169 LETIK--EFKPKVGCILNITPDHLDRHKTMENYIKAKARIFenqRPSDYTVLNYDDPRTRSLAKKAKARVIFFSRKSLle 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818551063 185 -----------ADFNPKRLPL----RLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRMNEVD 242
Cdd:PRK14106 247 egvfvkngkivISLGGKEEEVididEIFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFVA 319
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
234-317 |
4.35e-21 |
|
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: 86.63 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 234 VPGRMNEVDLGQNFQVFIDFAHTPNALKEALKTLKsqiPNPKSKLITVFGSAGERDKAKRPLMGKIAAGIADVSILTAED 313
Cdd:pfam02875 1 VPGRLEVVGENNGVLVIDDYAHNPDAMEAALRALR---NLFPGRLILVFGGMGDRDAEFHALLGRLAAALADVVILTGDY 77
|
....
gi 818551063 314 PRRE 317
Cdd:pfam02875 78 PRAE 81
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
27-287 |
2.83e-15 |
|
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: 77.06 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 27 QLTVIGITGTDGKTTTVWMVYEILKNSGfKV--------SQIsslGAlvgtsrfdtgfhtttpsPWQIqkyLRkaVNLGN 98
Cdd:COG0770 99 NIPVIAITGSNGKTTTKEMLAAVLSTKG-KVlatpgnfnNEI---GV-----------------PLTL---LR--LPEDH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 99 KYFVLEA-TSHGLDQNRLA-FVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKVNFS---ILNFDDQSFDFLKSNVD 173
Cdd:COG0770 153 EFAVLEMgMNHPGEIAYLArIARPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLPPGgvaVLNADDPLLAALAERAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 174 GKIITYSAKSQADF------------------NPKRLPLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVP 235
Cdd:COG0770 233 ARVLTFGLSEDADVraedieldedgtrftlhtPGGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVK 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 818551063 236 GRMNEVDLGQNFQVfIDFAH--TPNALKEALKTLkSQIPNPKSKlITVFGSAGE 287
Cdd:COG0770 313 GRLEVIEGAGGVTL-IDDSYnaNPDSMKAALDVL-AQLPGGGRR-IAVLGDMLE 363
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
27-287 |
4.44e-12 |
|
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: 67.29 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 27 QLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTsrfdtgfhtttpsPWQIqkyLRkaVNLGNKYFVLE-- 104
Cdd:TIGR01143 73 SGKVIGITGSSGKTTTKEMLAAILSHKYKVFATPGNFNNEIGL-------------PLTL---LR--APGDHDYAVLEmg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 105 ATSHGLDQNRLAFVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKVNFS---ILNFDDQSFDFLKS-NVDGKIITYS 180
Cdd:TIGR01143 135 ASHPGEIAYLAEIAKPDIAVITNIGPAHLEGFGSLEGIAEAKGEILQGLKENgiaVINADDPAFADLAKrLPNRNILSFG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 181 AKSqADFNPK-------------------RLPLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRMnEV 241
Cdd:TIGR01143 215 FEG-GDFVAKdisysalgstsftlvapggEFEVSLPLLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRF-EV 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 818551063 242 DLGQNFQVFIDfahTPNALKEALKTLKSQIPNPKSKLITVFGSAGE 287
Cdd:TIGR01143 293 QTKNGLTLIDD---TYNANPDSMRAALDALARFPGKKILVLGDMAE 335
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
20-348 |
1.18e-10 |
|
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 62.69 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 20 YFNFPSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVSQISS--L----------GALVGTSRFDTGFhtttpspWQIQ 87
Cdd:TIGR01499 10 ALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSphLvsfneririnGEPISDEELAQAF-------EQVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 88 KYLRKAVN----------LGNKYF--------VLEA-------------------TSHGLD-QNRL-------AFVKFKI 122
Cdd:TIGR01499 83 PILESLSQqptyfelltlLAFLYFaqaqvdvaVLEVglggrldatnvieplvsviTSIGLDhTEILgdtleeiAWEKAGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 123 ------AVITNVTHEHLD--YHKSQKRylgaKAKLFR-KVNFSILNFDDQSFDFlksnvdgkiitysaksqADFNPKRLP 193
Cdd:TIGR01499 163 ikegvpIVTGEQEPEALNvlKKKAQEK----GAPLFVvGRDFNYSETDENYLSF-----------------SGANLFLEP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 194 LRLKIPGDYNLRNALAAAAAVSSL-----RIKKKKILSVLNNFgGVPGRMNEVDlGQNFQVFIDFAHTPNALKEALKTLK 268
Cdd:TIGR01499 222 LALSLLGDHQQENAALALAALEVLgkqnpKLSEEAIRQGLANT-IWPGRLEILS-EDNPNILLDGAHNPHSAEALAEWFK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 269 sqIPNPKSKLITVFGSAGERDKAK--RPLMGKIaagIADVSILTAEDPRREKVEDICKSIAEGfseGKKEGKDYHIIYDR 346
Cdd:TIGR01499 300 --KRFNGRPITLLFGALADKDAAAmlAPLKPVV---DKEVFVTPFDYPRADDAADLAAFAEET---GKSTVEDWREALEE 371
|
..
gi 818551063 347 AK 348
Cdd:TIGR01499 372 AL 373
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
29-271 |
8.56e-10 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 60.60 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 29 TVIGITGTDGKTTTVWMVYEIL----KNSGFKVSQISSLGaLVGTSrfdtgfhtttpspwqiqkylrkavnlGN-KYFVL 103
Cdd:PRK14573 105 ISILVSGSHGKTTVSSLITAIFqeakKDPSYAIGGLNQEG-LNGYS--------------------------GSsEYFVA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 104 EA-TSHGLDQNRLAfvkfKIAVITNVTHEHLDYHKSQKRYLGAKAKLF-RKVNFSILNFDDQSFDFLKSNVDGK------ 175
Cdd:PRK14573 158 EAdESDGSLKHYTP----EFSVITNIDNEHLSNFEGDRELLLASIQDFaRKVQQINKCFYNGDCPRLKGCLQGHsygfss 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 176 -----IITYSAKS-QADFNPKRL-----PLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRMNEVDLG 244
Cdd:PRK14573 234 scdlhILSYYQEGwRSYFSAKFLgvvyqDIELNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRRLERKNSS 313
|
250 260
....*....|....*....|....*..
gi 818551063 245 QNFQVFIDFAHTPNALKEALKTLKSQI 271
Cdd:PRK14573 314 ETFLFLEDYAHHPSEISCTLRAVRDAV 340
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
30-133 |
3.83e-09 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 58.63 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 30 VIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTSRFDTGfHTTTPspwqiqkylRKAVN-LGNK---YFVLEA 105
Cdd:PRK14016 482 IVAVTGTNGKTTTTRLIAHILKLSGKRVGMTTTDGVYIDGRLIDKG-DCTGP---------KSARRvLMNPdveAAVLET 551
|
90 100
....*....|....*....|....*...
gi 818551063 106 TSHGLDQNRLAFVKFKIAVITNVTHEHL 133
Cdd:PRK14016 552 ARGGILREGLAYDRCDVGVVTNIGEDHL 579
|
|
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
24-367 |
6.44e-08 |
|
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 54.34 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 24 PSRQLTVIGITGTDGKTTTVWMVYEILKNSGFKVsqisslgalvgtsrfdtGFHTttpSPwqiqkYL-----RKAVN--- 95
Cdd:COG0285 36 PQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRV-----------------GLYT---SP-----HLvrfneRIRINgep 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 96 LGNKYFV-----LEATSHGLDQNRL---------AFVKFK--------------------------IAVITNVTHEHLDY 135
Cdd:COG0285 91 ISDEELVealeeVEPAVEEVDAGPPtffevttaaAFLYFAeapvdvavlevglggrldatnvidplVSVITSIGLDHTDF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 136 ---------------------------HKSQKRYLGAKAK------LFRKVNFSILNFDDQSFDFlksnvDGKIITYsak 182
Cdd:COG0285 171 lgdtleeiarekagiikpgvpvvtgdqQPEALEVIEERAAelgaplYRAGRDFSVEEREGAVFSY-----QGPGGEY--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 183 sqadfnpKRLPLRLkiPGDYNLRNALA-----AAAAVSSLRIKKKKILSVLNNFgGVPGRMnEVdLGQNFQVFIDFAHTP 257
Cdd:COG0285 243 -------EDLPLPL--LGAHQAENAALalaalEALRELGLPISEEAIREGLANA-RWPGRL-EV-LSRGPLVILDGAHNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 258 NALKEALKTLKSQIPNPksKLITVFGSAgeRDKAKRPLMGKIAAGIADVSILTAEDPRREKVEDICKSIAEgfsegkkEG 337
Cdd:COG0285 311 AGARALAETLKELFPFR--KLHLVFGML--ADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAARE-------LG 379
|
410 420 430
....*....|....*....|....*....|
gi 818551063 338 KDYHIIYDRAKAITFAVNLAADGDIVSLFG 367
Cdd:COG0285 380 LRVEVAPDVEEALEAALELADPDDLILVTG 409
|
|
| F430_CfbE |
NF033197 |
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ... |
30-274 |
2.03e-07 |
|
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.
Pssm-ID: 467992 [Multi-domain] Cd Length: 419 Bit Score: 52.71 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 30 VIGITGTDGKTTTVWMVYEILKNSGfkVSQISSLGALVGTSRFDTGFHTTTPSpwQIQKYLRKAVNLGNK---YFVLEaT 106
Cdd:NF033197 94 FIEITGVKGKTTTAELLAHILSDEY--VLLHTSRGTERYPEGELSNKGSITPA--SILNALELAEEIGIDdygFLIFE-V 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 107 SHGLdqnrlaFVKFKIAVITNVTHehlDYH--KSQKRYLGAKAKLF--RKVNFSILNFDdqsfDFLKSNVDGKIITYSAK 182
Cdd:NF033197 169 SLGG------TGAGDVGIITNILE---DYPiaGGKRSASAAKLQSLknAKVGSINVADL----GIYINGKNKLVITVAGV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 183 SQADFNPKR-----LPLRLK--IPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGRMNEVDLGQNfqVFIDFAh 255
Cdd:NF033197 236 EILSKYPLRfkygnTEFEFNplLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAVKKEGGV--VIVDNI- 312
|
250 260
....*....|....*....|....*
gi 818551063 256 tpN------ALKEALKTLKSQIPNP 274
Cdd:NF033197 313 --NpglnvkAIEYALDDALELLGDG 335
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
21-279 |
1.77e-04 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 43.79 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 21 FNFPsrqltVIGITGTDGKTTTVWMVYEILKNSGFKVSQISSLGALVGTsrfdtgfhtttP-SPWQIQKylrkAVNLGnk 99
Cdd:PRK11930 105 FDIP-----VIGITGSNGKTIVKEWLYQLLSPDYNIVRSPRSYNSQIGV-----------PlSVWQLNE----EHELG-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 100 yfVLEA-TSHGLDQNRLA-FVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLFRKVNFSILNFDDQSFD--FLKSNVDGK 175
Cdd:PRK11930 163 --IFEAgISQPGEMEALQkIIKPTIGILTNIGGAHQENFRSIKQKIMEKLKLFKDCDVIIYNGDNELISscITKSNLTLK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 176 IITYSAKSQ--------ADFNPKRLPLRLKIPGDYN-----------LRNALAAAAAVSSLRIKKKKILSVLNNFGGVPG 236
Cdd:PRK11930 241 LISWSRKDPeaplyipfVEKKEDHTVISYTYKGEDFhfeipfiddasIENLIHCIAVLLYLGYSADQIQERMARLEPVAM 320
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 818551063 237 RMnEVDLGQNFQVFID--FAHTPNALKEALKTLKSQIPNPKSKLI 279
Cdd:PRK11930 321 RL-EVKEGINNCTLINdsYNSDLQSLDIALDFLNRRSQSKKKTLI 364
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
28-287 |
4.44e-04 |
|
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: 42.38 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 28 LTVIGITGTDGKTTTVWMVYEILknsgfkvSQISSLGALVGTS-RFDTgfHTTTP-SPWQIQKYLRKAVnlgnkyFVLEA 105
Cdd:PRK11929 603 LPVVAITGSNGKTTTKEMIAAIL-------AAWQGEDRVLATEgNFNN--EIGVPlTLLRLRAQHRAAV------FELGM 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 106 TSHGlDQNRLA-FVKFKIAVITNVTHEHLDYHKSQKRYLGAKAKLF---RKVNFSILNFDD-QSFDFLKSNVDGKIITYS 180
Cdd:PRK11929 668 NHPG-EIAYLAaIAAPTVALVTNAQREHQEFMHSVEAVARAKGEIIaalPEDGVAVVNGDDpYTAIWAKLAGARRVLRFG 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 181 AKSQAD-----------------------FNPKRLPLRLKIPGDYNLRNALAAAAAVSSLRIKKKKILSVLNNFGGVPGR 237
Cdd:PRK11929 747 LQPGADvyaekiakdisvgeaggtrcqvvTPAGSAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGR 826
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 818551063 238 MNEVDLGQNFQVFID-FAHTPNALKEALKTLkSQIPNPKSKLItvFGSAGE 287
Cdd:PRK11929 827 MQRRRLSCGTRIIDDtYNANPDSMRAAIDVL-AELPNGPRALV--LGDMLE 874
|
|
| poly_gGlu_PgsB |
TIGR04012 |
poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in ... |
31-134 |
2.77e-03 |
|
poly-gamma-glutamate synthase PgsB/CapB; Of four genes commonly found to be involved in biosynthesis and export of poly-gamma-glutamate, pgsB(capB) and pgsC(capC) are found to be involved in the synthesis per se. Members of this family are designated PgsB, a nomeclature that covers both cases in which the poly-gamma-glutamate is secreted and those in which it is retained to form capsular material.PgsB has been shown to have poly-gamma-glutamate activity by itself but is bound tightly by PgsC (TIGR04011). [Cell envelope, Other]
Pssm-ID: 188527 [Multi-domain] Cd Length: 366 Bit Score: 39.61 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551063 31 IGITGTDGKTTTVWMVYEILKNSGFKVsqissLGALVGTSR---FDTG-----FHTTTPSPWQIQKYLRKAVNLGNKYFV 102
Cdd:TIGR04012 18 IHVNGTRGKSTVTRLITAGLREGGYKV-----VGKTTGTDArmiYPDGsefpiFRPGGANIGEQKRVVKKAVKLKADALV 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 818551063 103 LEATSHGLD-----QNRLafVKFKIAVITNVTHEHLD 134
Cdd:TIGR04012 93 LECMAVQPDyqivfELKL--VKANIGVITNVREDHMD 127
|
|
| |
