|
Name |
Accession |
Description |
Interval |
E-value |
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
24-487 |
0e+00 |
|
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: 575.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 24 GFCLDSRKVEAGHIFIALNSFSQpeKTLQFAQNALDAGALIVISEAALGIEKE----WVCPEVRNLMGEWQKQYLQltDP 99
Cdd:COG0769 1 GITYDSRKVKPGDLFVALPGARV--DGHDFIAQAIARGAVAVVTEAPGALLAAgvpvIVVPDPRAALALLAAAFYG--HP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 100 TQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEAS 179
Cdd:COG0769 77 SQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSLTTPEALDLQRLLAEMVDAGVTHVVMEVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAAQNnpsqpKILT 258
Cdd:COG0769 157 SHALDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQlGPGGAAVINADDPYGRRLAAAAPA-----RVIT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 259 YSLtQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQ 338
Cdd:COG0769 232 YGL-KADADLRATDIELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 339 VIQ-DDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTENPEQI 417
Cdd:COG0769 311 RVDgGQGPTVIVDYAHTPDALENVLEALRPHTKGRLIVVFGCGGDRDRGKRPLMGEIAARLADVVIVTSDNPRSEDPAAI 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 418 FADMKQGIHFAQHTmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAA 487
Cdd:COG0769 391 IADILAGIPGAGKV-LVIPDRAEAIRYAIALAKPGDVVLIAGKGHETYQIIGGVKIPFDDREVAREALAE 459
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
21-488 |
0e+00 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 539.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 21 PFKGFCLDSRKVEAGHIFIALNSFSQPEktLQFAQNALDAGALIVISEAALGIEKEW---VCPEVRNLMGEWQKQYLQlt 97
Cdd:PRK00139 14 EITGLTYDSRKVKPGDLFVALPGHKVDG--RDFIAQAIANGAAAVVAEADGEAGTGVpviIVPDLRKALALLAAAFYG-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 98 DPTQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALE 177
Cdd:PRK00139 90 HPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELIPSGLTTPDALDLQRLLAELVDAGVTYAAME 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 178 ASSHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAvVINLDDAHANIMLDAAQnnpsqpkil 257
Cdd:PRK00139 170 VSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLFSELGLAA-VINADDEVGRRLLALPD--------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 258 TYSLTQASADYHIADLQYRLSGASFSLITPtgcyaVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRM 337
Cdd:PRK00139 240 AYAVSMAGADLRATDVEYTDSGQTFTLVTE-----VESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 338 QVIQDDER-LFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTENPEQ 416
Cdd:PRK00139 315 ERVDAGQGpLVIVDYAHTPDALEKVLEALRPHAKGRLICVFGCGGDRDKGKRPLMGAIAERLADVVIVTSDNPRSEDPAA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518215315 417 IFADMKQGIHfaqhtmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAAQ 488
Cdd:PRK00139 395 IIADILAGIY------DVIEDRAEAIRYAIAQAKPGDVVLIAGKGHEDYQIIGGVKIPFDDREVAREALAER 460
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
23-477 |
3.69e-153 |
|
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: 444.45 E-value: 3.69e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 23 KGFCLDSRKVEAGHIFIALNSfsQPEKTLQFAQNALDAGALIVISEAALGIEKEWVC----PEVRNLMGEWQKQYLQltD 98
Cdd:TIGR01085 5 TGLTLDSREVKPGDLFVAIKG--THVDGHDFIHDAIANGAVAVVVERDVDFYVAPVPviivPDLRHALSSLAAAFYG--H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 99 PTQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNL---TPSTHTTLDALQLQSALHDYAKQGASFVA 175
Cdd:TIGR01085 81 PSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDlikNPAALTTPEALTLQSTLAEMVEAGAQYAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 176 LEASSHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAqnnpsqP 254
Cdd:TIGR01085 161 MEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTELGLKRFaVINLDDEYGAQFVKRL------P 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 255 KILTYSLTQASADYHIADLQ-----YRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAG-FALDKLVQFVP 328
Cdd:TIGR01085 235 KDITVSAITQPADGRAQDIKitdsgYSFEGQQFTFETPAGEGHLHTPLIGRFNVYNLLAALATLLHLGgIDLEDIVAALE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 329 QLQGAPGRMQVIQ-DDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSD 407
Cdd:TIGR01085 315 KFRGVPGRMELVDgGQKFLVIVDYAHTPDALEKALRTLRKHKDGRLIVVFGCGGDRDRGKRPLMGAIAEQLADLVILTSD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 408 NPRTENPEQIFADMKQGIHFAQHTmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDD 477
Cdd:TIGR01085 395 NPRGEDPEQIIADILAGISEKEKV-VIIADRRQAIRYAISNAKAGDVVLIAGKGHEDYQIIGGETIPFDD 463
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
27-487 |
4.22e-139 |
|
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: 424.50 E-value: 4.22e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 27 LDSRKVEAGHIFIALNSFSQPEKtlQFAQNALDAGALIVISEA-------ALGIEKEWVcPEVRNLMGEWQKQYLqlTDP 99
Cdd:PRK11929 34 LDSREVQPGDLFVACRGAASDGR--AFIDQALARGAAAVLVEAegedqvaAADALVLPV-ADLRKALGELAARWY--GRP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 100 TQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEAS 179
Cdd:PRK11929 109 SEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGARLDGRLIPGSLTTPDAIILHRILARMRAAGADAVAMEAS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLF-KFKTLKAVVINLDDAHANIMLDAaqnNPSQPKILt 258
Cdd:PRK11929 189 SHGLEQGRLDGLRIAVAGFTNLTRDHLDYHGTMQDYEEAKAALFsKLPGLGAAVINADDPAAARLLAA---LPRGLKVG- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 259 YSLTQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQ 338
Cdd:PRK11929 265 YSPQNAGADVQARDLRATAHGQVFTLATPDGSYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRME 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 339 VIQDDER----LFVVDYAHTPDALIQVLTTLK---RHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRT 411
Cdd:PRK11929 345 RVGPTAGaqgpLVVVDYAHTPDALAKALTALRpvaQARNGRLVCVFGCGGDRDKGKRPEMGRIAAELADRVVVTSDNPRS 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518215315 412 ENPEQIFADMKQGIHfAQHTMHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAA 487
Cdd:PRK11929 425 EAPEAIIDQILAGIP-AGARVFVISDRAEAIRQAIWMAAPGDVILIAGKGHETYQEIGGRKLFFDDREWARRALLA 499
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
28-472 |
7.09e-73 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 238.78 E-value: 7.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 28 DSRKVEAGHIFIALNSFSQPEktlqFAQNALDAGALIVISEA--ALGIEKEWVcPEVRNLMGEWQKQYLQltDPTQPLRG 105
Cdd:PRK14022 40 DSRTADEGTLFFAKGAYFKHK----FLQNAITQGLKLYVSEKdyEVGIPQVIV-PDIKKAMSLIAMEFYD--NPQHKLKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEASSHGLEQ 185
Cdd:PRK14022 113 LAFTGTKGKTTAAYFAYHILKQLHKPAMLSTMNTTLDGETFFKSALTTPESLDLFKMMAEAVDNGMTHLIMEVSSQAYLV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 186 GRLNGCDLEIAVYSNLSRDHLDY--HGTLEAYAEAKALLFKFKtlKAVVINLDDAHANIMLDAAQNNPsqpkILTYSLTQ 263
Cdd:PRK14022 193 GRVYGLTFDVGVFLNITPDHIGPieHPTFEDYFYHKRLLMENS--KAVVVNSDMDHFSELLEQVTPQE----HDFYGIDS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 264 asadyhiaDLQYRLSGAsFSLIT---PTGCYAVQspLLGHFNVENLLASLIAAECAGFALDKLVQFVPQlQGAPGRMQVI 340
Cdd:PRK14022 267 --------ENQIMASNA-FSFEAtgkLAGTYDIQ--LIGKFNQENAMAAGLACLRLGASLEDIQKGIAQ-TPVPGRMEVL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 341 -QDDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHAN-PVILTSDNPRTENPEQIF 418
Cdd:PRK14022 335 tQSNGAKVFIDYAHNGDSLNKLIDVVEEHQKGKLILLLGAAGNKGESRRPDFGRVANRHPYlQVILTADDPNNEDPKMIT 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 518215315 419 ADMKQGIHfaqHTMHEIHDRREAIKFVVAQA-RSGDIVVIAGKGHENYQEIDGVR 472
Cdd:PRK14022 415 QEIASHIT---HPVEIIDDRAEAIKHAMSITeGPGDAVIIAGKGADAYQIVPGHR 466
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
108-313 |
2.52e-64 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 207.16 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 108 VTGTNGKTTISRLIAELITSQhhgCAVMGTTGNGILPnltpSTHTTLDALQLQSALHDYAKQGASFVALEASSHGLEQGR 187
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLA---GGVIGTIGTYIGK----SGNTTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGEGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 188 LNG-CDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAQNNPSqpKILTYSLtQAS 265
Cdd:pfam08245 74 LSGlLKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIaVINADDPYGAFLIAKLKKAGV--RVITYGI-EGE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518215315 266 ADYHIADLQYRLSGASFSLI-TPTGCYAVQSPLLGHFNVENLLASLIAA 313
Cdd:pfam08245 151 ADLRAANIELSSDGTSFDLFtVPGGELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
1-378 |
2.67e-38 |
|
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: 145.24 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 1 MSISFQQIHPIsIDAAWYTQP---FKGFCLDSRKVEAGHIFIALnsfsQPEKT--LQFAQNALDAGALIVISEAALGIEK 75
Cdd:COG0770 1 ILLTLAEIAEA-TGGRLIGDPdlvVTGVSTDSRKIKPGDLFVAL----KGERFdgHDFVAQALAKGAAAALVSRPLPADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 76 E-WVCPEVRNLMGEWQKQYLQLTDPtqPLrgIAVTGTNGKTTISRLIAELITSQHHGCAvmgTTGN-----GiLPnLTps 149
Cdd:COG0770 76 PlIVVDDTLKALQQLAAAHRARFNI--PV--IAITGSNGKTTTKEMLAAVLSTKGKVLA---TPGNfnneiG-VP-LT-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 150 thttldALQLQSAlHDYAkqgasfVaLEAS-SHGLEQGRLngCDL---EIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF 225
Cdd:COG0770 145 ------LLRLPED-HEFA------V-LEMGmNHPGEIAYL--ARIarpDIAVITNIGPAHLEGFGSLEGIARAKGEIFEG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 226 ktLKA---VVINLDDAHANIMLDAAQNnpsqpKILTYSLtQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFN 302
Cdd:COG0770 209 --LPPggvAVLNADDPLLAALAERAKA-----RVLTFGL-SEDADVRAEDIELDEDGTRFTLHTPGGELEVTLPLPGRHN 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518215315 303 VENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQVIQDDERLFVVD--YAHTPDALIQVLTTLKR-HVNGQLWAVFG 378
Cdd:COG0770 281 VSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLEVIEGAGGVTLIDdsYNANPDSMKAALDVLAQlPGGGRRIAVLG 359
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
27-459 |
1.28e-33 |
|
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: 131.62 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 27 LDSRKVEAGHIFIAL--NSFSqpekTLQFAQNALDAGAliviseAALGIEKEWVCPEV---------RNLMGEWQKQYLQ 95
Cdd:TIGR01143 1 TDSRAIKPGDLFIALkgERFD----GHDFVEQALAAGA------VAVVVDREVGPDNGlpqilvddtLEALQALARAKRA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 96 LTdptqPLRGIAVTGTNGKTTISRLIAELItsQHHGcAVMGTTGN-----GILPNLtpsthttldaLQLqSALHDYAkqg 170
Cdd:TIGR01143 71 KF----SGKVIGITGSSGKTTTKEMLAAIL--SHKY-KVFATPGNfnneiGLPLTL----------LRA-PGDHDYA--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 171 asFVALEASSHGlEQGRLngCDL---EIAVYSNLSRDHLDYHGTLEAYAEAKALLFK-FKTLKAVVINLDDAHaniMLDA 246
Cdd:TIGR01143 130 --VLEMGASHPG-EIAYL--AEIakpDIAVITNIGPAHLEGFGSLEGIAEAKGEILQgLKENGIAVINADDPA---FADL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 247 AQNNPsQPKILTYSLTqaSADYHIADLQYR-LSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQ 325
Cdd:TIGR01143 202 AKRLP-NRNILSFGFE--GGDFVAKDISYSaLGSTSFTLVAPGGEFEVSLPLLGRHNVMNALAAAALALELGIPLEEIAE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 326 FVPQLQGAPGRMQVIQDDERLFVVD-YAHTPDALIQVLTTLKrHVNGQLWAVFG----CGGDRDRGKRPLMTQAALDHAN 400
Cdd:TIGR01143 279 GLAELKLVKGRFEVQTKNGLTLIDDtYNANPDSMRAALDALA-RFPGKKILVLGdmaeLGEYSEELHAEVGRYANSLGID 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 518215315 401 PVILTSDNPRTEnpEQIFAdmKQGIHFAQHTmheihdrrEAIKFVVAQARSGDIVVIAG 459
Cdd:TIGR01143 358 LVFLVGEEAAVI--YDSFG--KQGKHFADKD--------ELLAFLKTLVRKGDVVLVKG 404
|
|
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
104-461 |
3.52e-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: 125.18 E-value: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 104 RGIAVTGTNGKTTISRLIAELItsQHHGC---AVMGttgnGILPNLTPSthttldalqlqsalhdyAKQGAS--FVAlEA 178
Cdd:COG0773 105 RSIAVAGTHGKTTTTSMLAHIL--EEAGLdptFLIG----GILNNFGTN-----------------ARLGDGdyFVA-EA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 179 ----SSHgleqgrlngcdL----EIAVYSNLSRDHLDYHGTLEAYAEA-KALLFKFKTLKAVVINLDDAHANIMLDAAqn 249
Cdd:COG0773 161 desdGSF-----------LhyspDIAVVTNIEADHLDIYGDLEAIKEAfHEFARNVPFYGLLVLCADDPGLRELLPRC-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 250 npsQPKILTYSLTqASADYHIADLQYRLSGASFSLITPTGCYA-VQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVP 328
Cdd:COG0773 228 ---GRPVITYGFS-EDADYRAENIRIDGGGSTFDVLRRGEELGeVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 329 QLQGAPGRMQVIQDDERLFVV-DYAHTPDALIQVLTTLKRHV-NGQLWAVFgcggdrdrgkRP---LMTQA-------AL 396
Cdd:COG0773 304 SFKGVKRRFELKGEVGGVTVIdDYAHHPTEIAATLAAAREKYpDRRLVAVF----------QPhrySRTRDfldefaeAL 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518215315 397 DHANPVILTSDNPRTENP------EQIFADMKQGIHFAQHtmheIHDRREAIKFVVAQARSGDIVVIAGKG 461
Cdd:COG0773 374 SLADEVILLDIYAAREKPipgvssEDLAEAIRKRGKDVVY----VPDLDELVEALAEIARPGDVVLTMGAG 440
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
106-455 |
5.20e-30 |
|
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: 121.73 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELItsQHHGC-AVMGttGN-GilpnlTPsthtTLDALqLQSALHDYakqgasfVALEASSHGL 183
Cdd:COG0771 108 IAITGTNGKTTTTTLIGHIL--KAAGLrVAVG--GNiG-----TP----LLDLL-LEPEPPDV-------YVLELSSFQL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 184 EqgRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAAqnnpsQPKILTYSLT 262
Cdd:COG0771 167 E--TTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANqTPDDYAVLNADDPLTRALAEEA-----KARVVPFSLK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 263 Q-ASADYHIAD--LQYRLSGASFslitptgCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQV 339
Cdd:COG0771 240 EpLEGGAGLEDgkLVDRASGEEL-------LPVDDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEF 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 340 I-QDDERLFVVD-YAHTPDALIQVLTTLKRHVngqlwaVFGCGGDrDRG--KRPLMtQAALDHANPVILT-SDNPRtenp 414
Cdd:COG0771 313 VaEINGVRFINDsKATNPDATLAALESFDGPV------VLIAGGL-DKGadFSPLA-PAVAERVKAVVLIgEDAEK---- 380
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 518215315 415 eqiFADMKQGIHFAqhtMHEIHDRREAIKFVVAQARSGDIV 455
Cdd:COG0771 381 ---IAAALAGAGVP---VVIVETMEEAVAAAAELARPGDVV 415
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
106-458 |
3.41e-28 |
|
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: 116.29 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELItsQHHGC-AVMGttGN-GILPnltpsthttLDALqlqsalhdyAKQGASFVALEASSHGL 183
Cdd:TIGR01087 105 VAITGTNGKTTTTSLLYHLL--KAAGLkAFLG--GNiGTPA---------LEVL---------DQEGAELYVLELSSFQL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 184 EqgRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHAnimldAAQNNPSQPKILTYSLT 262
Cdd:TIGR01087 163 E--TTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVaVLNADDPRF-----ARLAQKSKAQVIWFSVE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 263 QAsADYHIADLQYRLSGASFSLItptgcyavqSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQVI-Q 341
Cdd:TIGR01087 236 KD-AERGLCIRDGGLYLKPNDLE---------GSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVgQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 342 DDERLFVVDYAHT-PDALIQVLTTLKRHVNgqlWAVfgCGGDRDRGKRPLMTQAALDHANPVILTSDNPrtenpeQIFAD 420
Cdd:TIGR01087 306 KNGVHFYNDSKATnVHATLAALSAFDNPVI---LIV--GGDDKGADFSPLAPAAAGKVKAVLAIGEDAA------KIAPL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 518215315 421 MKQGIHFAQ--HTMheihdrREAIKFVVAQARSGDIVVIA 458
Cdd:TIGR01087 375 LKEAGLSVYlvESL------EEAVQAAREVASPGDVVLLS 408
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
334-418 |
1.87e-23 |
|
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: 93.95 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 334 PGRMQVIQDDER-LFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTE 412
Cdd:pfam02875 2 PGRLEVVGENNGvLVIDDYAHNPDAMEAALRALRNLFPGRLILVFGGMGDRDAEFHALLGRLAAALADVVILTGDYPRAE 81
|
....*.
gi 518215315 413 NPEQIF 418
Cdd:pfam02875 82 DPGAII 87
|
|
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
96-459 |
7.52e-23 |
|
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: 100.56 E-value: 7.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 96 LTDPTQPLRGIAVTGTNGKTTISRLIAELItsQHHGCavmgTTG------------------------------------ 139
Cdd:COG0285 33 LGNPQRKLPVIHVAGTNGKGSTAAMLESIL--RAAGY----RVGlytsphlvrfneriringepisdeelvealeevepa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 140 NGILPNLTPST--HTTLDALQLqsalhdYAKQGASFVALEAsshGLEqGRL---NGCDLEIAVYSNLSRDHLDYHG-TLE 213
Cdd:COG0285 107 VEEVDAGPPTFfeVTTAAAFLY------FAEAPVDVAVLEV---GLG-GRLdatNVIDPLVSVITSIGLDHTDFLGdTLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 214 AYAEAKALLFKFKTlKAVVINLDDAHANIMLDAAQNNPSQpkiltysLTQASADYHIADLQyrlsGASFSLITPTGCYA- 292
Cdd:COG0285 177 EIAREKAGIIKPGV-PVVTGDQQPEALEVIEERAAELGAP-------LYRAGRDFSVEERE----GAVFSYQGPGGEYEd 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 293 VQSPLLGHFNVENLLASLIAAEcagfALDKLVQFVPQ------LQGA--PGRMQVIQDDeRLFVVDYAHTPDALIQVLTT 364
Cdd:COG0285 245 LPLPLLGAHQAENAALALAALE----ALRELGLPISEeairegLANArwPGRLEVLSRG-PLVILDGAHNPAGARALAET 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 365 LKRH-VNGQLWAVFGCGGDRDRGKrplMTQAALDHANPVILTS-DNPRTENPEQIFADMKQgihfAQHTMHEIHDRREAI 442
Cdd:COG0285 320 LKELfPFRKLHLVFGMLADKDIEG---MLAALAPLADEVIVTTpPSPRALDAEELAEAARE----LGLRVEVAPDVEEAL 392
|
410
....*....|....*..
gi 518215315 443 KFVVAQARSGDIVVIAG 459
Cdd:COG0285 393 EAALELADPDDLILVTG 409
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
28-367 |
4.29e-22 |
|
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: 100.16 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 28 DSRKVEAGHIFIAL--NSFSQPEktlqFAQNALDAGAliviseAALGIEKEW--------VCPEVRNLMGEWQKQYL-QL 96
Cdd:PRK11929 532 DSRSVGRGELFVALrgENFDGHD----YLPQAFAAGA------CAAVVERQVadvdlpqiVVDDTRAALGRLATAWRaRF 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 97 TDPTqplrgIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNgiLPNLT--PsthttLDALQLQsalhdyAKQGASFV 174
Cdd:PRK11929 602 SLPV-----VAITGSNGKTTTKEMIAAILAAWQGEDRVLATEGN--FNNEIgvP-----LTLLRLR------AQHRAAVF 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 175 ALEASSHGlEQGRLNG-CDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAqnnpS 252
Cdd:PRK11929 664 ELGMNHPG-EIAYLAAiAAPTVALVTNAQREHQEFMHSVEAVARAKGEIIAALPEDGVaVVNGDDPYTAIWAKLA----G 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 253 QPKILTYSLTQASADYH---IADLQ-YRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVP 328
Cdd:PRK11929 739 ARRVLRFGLQPGADVYAekiAKDISvGEAGGTRCQVVTPAGSAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLE 818
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 518215315 329 QLQGAPGRMQVIQDDERLFVVD--YAHTPDAL---IQVLTTLKR 367
Cdd:PRK11929 819 RFQPVAGRMQRRRLSCGTRIIDdtYNANPDSMraaIDVLAELPN 862
|
|
| cya_phycin_syn |
TIGR02068 |
cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and ... |
106-474 |
2.90e-21 |
|
cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and energy, found in most Cyanobacteria. The polymer has a backbone of L-aspartic acid, with most Asp side chain carboxyl groups attached to L-arginine. The polymer is made by this enzyme, cyanophycin synthetase, and degraded by cyanophycinase. Heterologously expressed cyanophycin synthetase in E. coli produces a closely related, water-soluble polymer with some Arg replaced by Lys. It is unclear whether enzymes that produce soluble cyanophycin-like polymers in vivo in non-Cyanobacterial species should be designated as cyanophycin synthetase itself or as a related enzyme. This model makes the designation as cyanophycin synthetase. Cyanophycin synthesis is analogous to polyhydroxyalkanoic acid (PHA) biosynthesis, except that PHA polymers lack nitrogen and may be made under nitrogen-limiting conditions. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 273950 [Multi-domain] Cd Length: 864 Bit Score: 97.54 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELItsQHHGCAVMGTTGNGIL---------PNLTPST------HTTLDALQLQSALHDYAKQG 170
Cdd:TIGR02068 482 VSVTGTNGKTTTTRLVAHIL--KQTGKVVGMTTTDGVYigkylvekgDNTGPASarrilmDPTVDAAVLETARGGILREG 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 171 ASFvaleasshgleqgrlNGCDleIAVYSNLSRDHL--DYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAA 247
Cdd:TIGR02068 560 LAF---------------DRCD--VGVVTNIAGDHLgiGDINTIEDLADVKRVVVEVvLPDGYAVLNADDPMVAAMAEKC 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 248 QN-------NPSQPKILTYSLTQASADYHIADlqyRLSGASFSLITPTGcYAVQSPL-LGH---FNVENLLASLIAAECA 316
Cdd:TIGR02068 623 KGkiayfsmDPNNPTVAAHIADGGRAVYYENG---YIVIARGGDEVAIA-RIAAIPLtMGGrvaFQIENALAAVAAAWAL 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 317 GFALDKLVQ----FVPQLQGAPGRMQVIQDDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMT 392
Cdd:TIGR02068 699 GVPIELIRAgirtFDADAAQAPGRFNLFNLGGAHVLVDYGHNPAAIEAVGAAIRNWPARRRIGVIGGPGDRRDEDLVEQG 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 393 QAALDHANPVILTSDNPRTENPE-QIFADMKQGIHFAQHTMH--EIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEID 469
Cdd:TIGR02068 779 ELLGGAFDQIILKEDDDVRGRPRgEAAALLRQGLRQSARKAAieDILDETEAIAAALDDLRAGDLVVIFPESVERAIKLI 858
|
....*
gi 518215315 470 GVRHW 474
Cdd:TIGR02068 859 LVRVW 863
|
|
| murF |
PRK10773 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed |
28-350 |
5.99e-19 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
Pssm-ID: 182718 [Multi-domain] Cd Length: 453 Bit Score: 89.32 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 28 DSRKVEAGHIFIALnsfsQPEK--TLQFAQNALDAGALIVISEAALGIEkewvCPEV-----RNLMGE---WQKQylqlt 97
Cdd:PRK10773 30 DTRKVTPGCLFVAL----KGERfdAHDFADDAKAAGAGALLVSRPLDID----LPQLvvkdtRLAFGQlaaWVRQ----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 98 dpTQPLRGIAVTGTNGKTTISRLIAElITSQhhgCA-VMGTTGN-----GI---LPNLTPSthttldalqlqsalHDYA- 167
Cdd:PRK10773 97 --QVPARVVALTGSSGKTSVKEMTAA-ILRQ---CGnTLYTAGNlnndiGVpltLLRLTPE--------------HDYAv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 168 -KQGASFVALEASSHGLEQGrlngcdlEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAVVI-NLDD---AHAni 242
Cdd:PRK10773 157 iELGANHQGEIAYTVSLTRP-------EAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAImNADSndwLNW-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 243 mldaaQNNPSQPKILTYSLTQA-SADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALD 321
Cdd:PRK10773 228 -----QSVIGSKTVWRFSPNAAnSVDFTATNIHVTSHGTEFTLHTPTGSVDVLLPLPGRHNIANALAAAALAMSVGATLD 302
|
330 340
....*....|....*....|....*....
gi 518215315 322 KLVQFVPQLQGAPGRMQVIQDDERLFVVD 350
Cdd:PRK10773 303 AVKAGLANLKAVPGRLFPIQLAEGQLLLD 331
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
104-461 |
4.72e-15 |
|
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: 77.35 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 104 RGIAVTGTNGKTTISRLIAELItsQHHG---CAVMGttgnGILPNLTPSTHTtldalqlqsalhdyaKQGASFV--ALEA 178
Cdd:TIGR01082 100 HSIAVAGTHGKTTTTAMIAVIL--KEAGldpTVVVG----GLVKEAGTNARL---------------GSGEYLVaeADES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 179 SSHGLEQGRlngcdlEIAVYSNLSRDHLD-YHGTLEAYAEAkalLFKF----KTLKAVVINLDDAHANIMLDAAQNnpsq 253
Cdd:TIGR01082 159 DASFLHLQP------NVAIVTNIEPDHLDtYGSSFERLKAA---FEKFihnlPFYGLAVICADDPVLRELVPKATE---- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 254 pKILTYSLTQASADYHIADLQYRLSGASFSLITP-TGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQG 332
Cdd:TIGR01082 226 -QVITYGGSGEDADYRAENIQQSGAEGKFSVRGKgKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 333 APGRMQVIQDDERLFVVD-YAHTPDALIQVLTTLKRHVNGQ-LWAVFgcggdrdRGKRPLMTQA-------ALDHANPVI 403
Cdd:TIGR01082 305 VKRRFEILGEFGGVLLIDdYAHHPTEIKATLKAARQGYPDKrIVVVF-------QPHRYSRTRDlfddfakVLSDADELI 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518215315 404 LTSDNPRTENP------EQIFADMKQGIHFaqhTMHEIHDRREAIKFVVAQARSGDIVVIAGKG 461
Cdd:TIGR01082 378 LLDIYAAGEEPingidgKSLARKITQLGKI---EPYFVPDLAELVEFLAAVLQSGDLILTMGAG 438
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
106-367 |
8.29e-13 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 70.38 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGngilpnltpsthttldaLQLQSALHDYAKQGAsFVAlEASSHGLE- 184
Cdd:PRK14106 111 VAITGTNGKTTTTTLLGEIFKNAGRKTLVAGNIG-----------------YPLIDAVEEYGEDDI-IVA-EVSSFQLEt 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 185 --QGRLNgcdleIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKA-VVINLDDAhanIMLDAAQNNPSQpkILTYSL 261
Cdd:PRK14106 172 ikEFKPK-----VGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDyTVLNYDDP---RTRSLAKKAKAR--VIFFSR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 262 TqasadyHIADLQYRLSGASFSLITPTGCYAVQS----PLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRM 337
Cdd:PRK14106 242 K------SLLEEGVFVKNGKIVISLGGKEEEVIDideiFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRI 315
|
250 260 270
....*....|....*....|....*....|..
gi 518215315 338 QVIQDDER-LFVVDYAHT-PDALIQVLTTLKR 367
Cdd:PRK14106 316 EFVAEINGvKFINDSKGTnPDAAIKALEAYET 347
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
91-384 |
3.59e-09 |
|
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: 58.45 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 91 KQYLQ-LTDPTQPLRGIAVTGTNGKTTISRLIAELI----------TSQHhgcaVMGTTG----NGIlpNLTPSTHT--- 152
Cdd:TIGR01499 5 KKLLEaLGNPQDLYPVIHVAGTNGKGSTCAFLESILraagykvglfTSPH----LVSFNEririNGE--PISDEELAqaf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 153 -----TLDALQLQ---------SALHDYAKQGASFVALEAsshGLeQGRL---NGCDLEIAVYSNLSRDHLDYHG-TLEA 214
Cdd:TIGR01499 79 eqvrpILESLSQQptyfelltlLAFLYFAQAQVDVAVLEV---GL-GGRLdatNVIEPLVSVITSIGLDHTEILGdTLEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 215 YAEAKALLFKFKTlKAVVINLDDAHANIMLDAAQNNPSQpkiltysLTQASADYHI--ADLQYRLSGASFSLITPtgcya 292
Cdd:TIGR01499 155 IAWEKAGIIKEGV-PIVTGEQEPEALNVLKKKAQEKGAP-------LFVVGRDFNYseTDENYLSFSGANLFLEP----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 293 VQSPLLGHFNVENLLASLIAAECAGFALDKL-VQFVPQ-LQGA--PGRMQVIQDDERLFVVDYAHTPDALIQVLTTLKRH 368
Cdd:TIGR01499 222 LALSLLGDHQQENAALALAALEVLGKQNPKLsEEAIRQgLANTiwPGRLEILSEDNPNILLDGAHNPHSAEALAEWFKKR 301
|
330
....*....|....*..
gi 518215315 369 VNGQ-LWAVFGCGGDRD 384
Cdd:TIGR01499 302 FNGRpITLLFGALADKD 318
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
106-339 |
5.14e-09 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 58.63 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELITSQHHgcaVMG-TTGNGILPN--LTPSTHTTldalQLQSA---LHDYAKQGAsfvALEAS 179
Cdd:PRK14016 483 VAVTGTNGKTTTTRLIAHILKLSGK---RVGmTTTDGVYIDgrLIDKGDCT----GPKSArrvLMNPDVEAA---VLETA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHG-LEQGrL--NGCDleIAVYSNLSRDHLDYHG--TLEAYAEAKALLFK-FKTLKAVVINLDDAHANIMLDAAQN---- 249
Cdd:PRK14016 553 RGGiLREG-LayDRCD--VGVVTNIGEDHLGLGGinTLEDLAKVKRVVVEaVKPDGYAVLNADDPMVAAMAERCKGkvif 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 250 ---NPSQPKILTY---------------SLTQASADYHIADLqyrlsgasfSLITPTgcyavqspLLGH--FNVENLLAS 309
Cdd:PRK14016 630 fsmDPDNPVIAEHraqggravyvegdyiVLAEGGWEIRIISL---------ADIPLT--------LGGKagFNIENALAA 692
|
250 260 270
....*....|....*....|....*....|....
gi 518215315 310 LIAAECAGFALDK----LVQFVPQLQGAPGRMQV 339
Cdd:PRK14016 693 IAAAWALGIDIELiragLRTFVSDAAQAPGRFNL 726
|
|
|