|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
3-422 |
2.34e-158 |
|
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: 453.02 E-value: 2.34e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 3 ETYEQALAFIHGRHKWTKTPTFDRLGFILATLNHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFN 82
Cdd:COG0285 2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 83 ERIQDNNGPISDAQLLTLVQRLEPLVRAQDVAHPgfelTEFEIVTVLMFMYFEQMPVDVVILEVGIGGMWDSTQIIaDKL 162
Cdd:COG0285 82 ERIRINGEPISDEELVEALEEVEPAVEEVDAGPP----TFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI-DPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 163 AAVITSVSYDHMHVLGDTLTEITQQKADIIAPGKPVIVGDLPQEALTVVQDIAQKRDSDLYVYGQSFGMRTVDHQ-LTYV 241
Cdd:COG0285 157 VSVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEEREGAvFSYQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 242 IDQHKLP-VQLNLNGQYQIGNAAVAIKTVQtVAPMLGVTIADAAIQEGLRHVIWPARFETVADHPLVIVDGAHNVAGIDA 320
Cdd:COG0285 237 GPGGEYEdLPLPLLGAHQAENAALALAALE-ALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAGARA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 321 LVQTLRSSYGDKTVGIVFSALADKHFEQMLRHLLAETNlKIVVVPFtaPGSR----QAIAGLPFTH-PRLTWGDDWQTAL 395
Cdd:COG0285 316 LAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLAD-EVIVTTP--PSPRaldaEELAEAARELgLRVEVAPDVEEAL 392
|
410 420 430
....*....|....*....|....*....|
gi 917632672 396 KSLQAQT---DMTVITGSLYFVSEVRQQFK 422
Cdd:COG0285 393 EAALELAdpdDLILVTGSLYLVGEVRALLG 422
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
24-419 |
1.66e-122 |
|
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: 361.22 E-value: 1.66e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 24 FDRLGFILATLNHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFNERIQDNNGPISDAQLLTLVQR 103
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 104 LEPLVRAQDvahpgFELTEFEIVTVLMFMYFEQMPVDVVILEVGIGGMWDSTQIIaDKLAAVITSVSYDHMHVLGDTLTE 183
Cdd:TIGR01499 81 VRPILESLS-----QQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVI-EPLVSVITSIGLDHTEILGDTLEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 184 ITQQKADIIAPGKPVIVGDLPQEALTVVQDIAQKRDSDLYVYGQSFGMRTVDHQLTYVIDQH--KLPVQLNLNGQYQIGN 261
Cdd:TIGR01499 155 IAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYLSFSGANlfLEPLALSLLGDHQQEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 262 AAVAIKTVQTVAPmLGVTIADAAIQEGLRHVIWPARFETVA-DHPLVIVDGAHNVAGIDALVQTLRSSYGDKTVGIVFSA 340
Cdd:TIGR01499 235 AALALAALEVLGK-QNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 341 LADKHFEQMLRHLLAETNLKIVVVPFTAPGS------RQAIAGLPFthprlTWGDDWQTALKSLQA--QTDMTVITGSLY 412
Cdd:TIGR01499 314 LADKDAAAMLAPLKPVVDKEVFVTPFDYPRAddaadlAAFAEETGK-----STVEDWREALEEALNasAEDDILVTGSLY 388
|
....*..
gi 917632672 413 FVSEVRQ 419
Cdd:TIGR01499 389 LVGEVRK 395
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
25-417 |
5.61e-49 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 171.80 E-value: 5.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 25 DRLGFILATLNHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFNERIQDNNGPISDAQLLTLVQRL 104
Cdd:PRK10846 33 ERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTASFAEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 105 EplvraqdVAHPGFELTEFEIVTVLMFMYFEQMPVDVVILEVGIGGMWDSTQIIaDKLAAVITSVSYDHMHVLGDTLTEI 184
Cdd:PRK10846 113 E-------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIV-DADVAVVTSIALDHTDWLGPDRESI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 185 TQQKADIIAPGKPVIVG--DLPQEALTVVQDIA---QKRDSD--LYVYGQSFGMRTVDHQLTyvidqhKLPVQlnlngQY 257
Cdd:PRK10846 185 GREKAGIFRAEKPAVVGepDMPSTIADVAQEKGallQRRGVDwnYSVTDHDWAFSDGDGTLE------NLPLP-----NV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 258 QIGNAAVAIKTVQTVapmlGVTIADAAIQEGLRHVIWPARFETVADHPLVIVDGAHNVAGIDALVQTLRSSYGDKTVGIV 337
Cdd:PRK10846 254 PLPNAATALAALRAS----GLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKALPKNGRVLAV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 338 FSALADKHFEQMLRHLLAEtnlkiVVVPFTAP--GSRQAIAGLPFTHprLTWG---DD----WQTALKSLQAQtDMTVIT 408
Cdd:PRK10846 330 IGMLHDKDIAGTLACLKSV-----VDDWYCAPleGPRGATAEQLAEH--LGNGksfDSvaqaWDAAMADAKPE-DTVLVC 401
|
....*....
gi 917632672 409 GSLYFVSEV 417
Cdd:PRK10846 402 GSFHTVAHV 410
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
294-365 |
1.85e-07 |
|
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: 48.49 E-value: 1.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917632672 294 WPARFE--TVADHPLVIVDGAHNVAGIDALVQTLRSSYGDKTVgIVFSALADK--HFEQMLRHLLAETNLKIVVVP 365
Cdd:pfam02875 1 VPGRLEvvGENNGVLVIDDYAHNPDAMEAALRALRNLFPGRLI-LVFGGMGDRdaEFHALLGRLAAALADVVILTG 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
3-422 |
2.34e-158 |
|
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: 453.02 E-value: 2.34e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 3 ETYEQALAFIHGRHKWTKTPTFDRLGFILATLNHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFN 82
Cdd:COG0285 2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 83 ERIQDNNGPISDAQLLTLVQRLEPLVRAQDVAHPgfelTEFEIVTVLMFMYFEQMPVDVVILEVGIGGMWDSTQIIaDKL 162
Cdd:COG0285 82 ERIRINGEPISDEELVEALEEVEPAVEEVDAGPP----TFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI-DPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 163 AAVITSVSYDHMHVLGDTLTEITQQKADIIAPGKPVIVGDLPQEALTVVQDIAQKRDSDLYVYGQSFGMRTVDHQ-LTYV 241
Cdd:COG0285 157 VSVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEEREGAvFSYQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 242 IDQHKLP-VQLNLNGQYQIGNAAVAIKTVQtVAPMLGVTIADAAIQEGLRHVIWPARFETVADHPLVIVDGAHNVAGIDA 320
Cdd:COG0285 237 GPGGEYEdLPLPLLGAHQAENAALALAALE-ALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAGARA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 321 LVQTLRSSYGDKTVGIVFSALADKHFEQMLRHLLAETNlKIVVVPFtaPGSR----QAIAGLPFTH-PRLTWGDDWQTAL 395
Cdd:COG0285 316 LAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLAD-EVIVTTP--PSPRaldaEELAEAARELgLRVEVAPDVEEAL 392
|
410 420 430
....*....|....*....|....*....|
gi 917632672 396 KSLQAQT---DMTVITGSLYFVSEVRQQFK 422
Cdd:COG0285 393 EAALELAdpdDLILVTGSLYLVGEVRALLG 422
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
24-419 |
1.66e-122 |
|
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: 361.22 E-value: 1.66e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 24 FDRLGFILATLNHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFNERIQDNNGPISDAQLLTLVQR 103
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 104 LEPLVRAQDvahpgFELTEFEIVTVLMFMYFEQMPVDVVILEVGIGGMWDSTQIIaDKLAAVITSVSYDHMHVLGDTLTE 183
Cdd:TIGR01499 81 VRPILESLS-----QQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVI-EPLVSVITSIGLDHTEILGDTLEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 184 ITQQKADIIAPGKPVIVGDLPQEALTVVQDIAQKRDSDLYVYGQSFGMRTVDHQLTYVIDQH--KLPVQLNLNGQYQIGN 261
Cdd:TIGR01499 155 IAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYLSFSGANlfLEPLALSLLGDHQQEN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 262 AAVAIKTVQTVAPmLGVTIADAAIQEGLRHVIWPARFETVA-DHPLVIVDGAHNVAGIDALVQTLRSSYGDKTVGIVFSA 340
Cdd:TIGR01499 235 AALALAALEVLGK-QNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 341 LADKHFEQMLRHLLAETNLKIVVVPFTAPGS------RQAIAGLPFthprlTWGDDWQTALKSLQA--QTDMTVITGSLY 412
Cdd:TIGR01499 314 LADKDAAAMLAPLKPVVDKEVFVTPFDYPRAddaadlAAFAEETGK-----STVEDWREALEEALNasAEDDILVTGSLY 388
|
....*..
gi 917632672 413 FVSEVRQ 419
Cdd:TIGR01499 389 LVGEVRK 395
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
25-417 |
5.61e-49 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 171.80 E-value: 5.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 25 DRLGFILATLNHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFNERIQDNNGPISDAQLLTLVQRL 104
Cdd:PRK10846 33 ERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTASFAEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 105 EplvraqdVAHPGFELTEFEIVTVLMFMYFEQMPVDVVILEVGIGGMWDSTQIIaDKLAAVITSVSYDHMHVLGDTLTEI 184
Cdd:PRK10846 113 E-------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIV-DADVAVVTSIALDHTDWLGPDRESI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 185 TQQKADIIAPGKPVIVG--DLPQEALTVVQDIA---QKRDSD--LYVYGQSFGMRTVDHQLTyvidqhKLPVQlnlngQY 257
Cdd:PRK10846 185 GREKAGIFRAEKPAVVGepDMPSTIADVAQEKGallQRRGVDwnYSVTDHDWAFSDGDGTLE------NLPLP-----NV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 258 QIGNAAVAIKTVQTVapmlGVTIADAAIQEGLRHVIWPARFETVADHPLVIVDGAHNVAGIDALVQTLRSSYGDKTVGIV 337
Cdd:PRK10846 254 PLPNAATALAALRAS----GLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKALPKNGRVLAV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 338 FSALADKHFEQMLRHLLAEtnlkiVVVPFTAP--GSRQAIAGLPFTHprLTWG---DD----WQTALKSLQAQtDMTVIT 408
Cdd:PRK10846 330 IGMLHDKDIAGTLACLKSV-----VDDWYCAPleGPRGATAEQLAEH--LGNGksfDSvaqaWDAAMADAKPE-DTVLVC 401
|
....*....
gi 917632672 409 GSLYFVSEV 417
Cdd:PRK10846 402 GSFHTVAHV 410
|
|
| PLN02913 |
PLN02913 |
dihydrofolate synthetase |
24-420 |
3.01e-46 |
|
dihydrofolate synthetase
Pssm-ID: 178501 [Multi-domain] Cd Length: 510 Bit Score: 166.53 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 24 FD--RLGFILATLNHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFNERIQDNN--GPISDAQLLT 99
Cdd:PLN02913 56 FDlgRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGKlgKPVSTNTLND 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 100 LVQRLEPLVRaQDVAHPGFELTEFEIVTVLMFMYFEQMPVDVVILEVGIGGMWDSTQII-ADKLAA-VITSVSYDHMHVL 177
Cdd:PLN02913 136 LFHGIKPILD-EAIQLENGSLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIdSSGLAAsVITTIGEEHLAAL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 178 GDTLTEITQQKADIIAPGKPVIVGdlpQEALTVVQDIAQKRDS----------DLYVYGQSFGMRTVD---HQLTYVIDQ 244
Cdd:PLN02913 215 GGSLESIALAKSGIIKQGRPVVLG---GPFLPHIESILRDKASsmnspvvsasDPGVRSSIKGIITDNgkpCQSCDIVIR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 245 HKLPVQLNLN---------GQYQIGNAAVAIktvqTVAPML---GVTIADAAIQEGLRHVIWPARFETVADHPL------ 306
Cdd:PLN02913 292 VEKDDPLFIElsdvnlrmlGSHQLQNAVTAA----CAALCLrdqGWRISDASIRAGLENTNLLGRSQFLTSKEAevlglp 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 307 ---VIVDGAHNVAGIDALVQTLRSSYGDKTVGIVFSALADKHFEQMLRHLLAETNLKIVVV-----------PFTAP--- 369
Cdd:PLN02913 368 gatVLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKDHLAFASEFLSGLKPEAVFLteadiaggksrSTSASalk 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917632672 370 ----------GSRQAIAGLPFTHPRLTWGDdwQTALKS-LQAQTDMTVITGSLYFVSEVRQQ 420
Cdd:PLN02913 448 eawikaapelGIETLLAENNSLLKSLVDAS--AILRKArTLDPSSVVCVTGSLHIVSAVLAS 507
|
|
| PLN02881 |
PLN02881 |
tetrahydrofolylpolyglutamate synthase |
3-313 |
6.25e-42 |
|
tetrahydrofolylpolyglutamate synthase
Pssm-ID: 215476 Cd Length: 530 Bit Score: 155.20 E-value: 6.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 3 ETYEQAL----AFIHGR---HKWTKTPTFDRLGFILATLNHPEH--KQKYIHVTGTNGKGSTSQMMASILRAANLQVGLF 73
Cdd:PLN02881 14 DSYEEALdalsSLITKKsraDPSNPGDQFDLLFDYLKILELEEAisRLKVIHVAGTKGKGSTCTFTESILRNCGFRTGLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 74 SSPFI----ERFneRIqdnNG-PISDAQLLT----LVQRLEPLVrAQDVAHPGFelteFEIVTVLMFMYFEQMPVDVVIL 144
Cdd:PLN02881 94 TSPHLidvrERF--RL---DGvDISEEKFLRyfwwCWDRLKEKT-TEDLPMPAY----FRFLTLLAFKIFSAEQVDVAIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 145 EVGIGGMWDSTQIIADKLAAVITSVSYDHMHVLGDTLTEITQQKADIIAPGKPVIVGDLPQEALTVVQDIAQKRDSDLyv 224
Cdd:PLN02881 164 EVGLGGRLDATNVVQKPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAFTVPQPDEAMRVLEERASELGVPL-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 225 ygqsfgmrTVDHQLtyviDQHKL-PVQLNLNGQYQIGNAAVAIKTVQTVAPMLGVTIADAAIQE---------GLRHVIW 294
Cdd:PLN02881 242 --------QVVEPL----DSYGLsGLKLGLAGEHQYLNAGLAVALCSTWLQRTGHEEFEALLQAgtlpeqfikGLSTASL 309
|
330 340
....*....|....*....|....*...
gi 917632672 295 PARFETVADHPLVI---------VDGAH 313
Cdd:PLN02881 310 QGRAQVVPDSYINSedsgdlvfyLDGAH 337
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
35-327 |
8.90e-12 |
|
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: 66.57 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 35 NHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSPFIERFNERIqdnngpisdaqlltlvqrleplvrAQDVA 114
Cdd:TIGR01085 79 GHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDL------------------------IKNPA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 115 HpgfeLTEFEIVTVLMFMY-FEQMPVDVVILEVGIGGMWDSTQIIADKLAAVITSVSYDHMHVLGdTLTEITQQKA---- 189
Cdd:TIGR01085 135 A----LTTPEALTLQSTLAeMVEAGAQYAVMEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHG-TMENYFAAKAslft 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 190 DIIAPGKPVI----------VGDLPQEalTVVQDIAQKRDS---DLYVYgqSFGMRTVDHQLTYVIDQHKLPVQLNLNGQ 256
Cdd:TIGR01085 210 ELGLKRFAVInlddeygaqfVKRLPKD--ITVSAITQPADGraqDIKIT--DSGYSFEGQQFTFETPAGEGHLHTPLIGR 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917632672 257 YQIGNAAVAIKTVQTVapmLGVTIADaaIQEGLRHVIW-PARFETV--ADHPLVIVDGAHNvagIDALVQTLRS 327
Cdd:TIGR01085 286 FNVYNLLAALATLLHL---GGIDLED--IVAALEKFRGvPGRMELVdgGQKFLVIVDYAHT---PDALEKALRT 351
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
35-326 |
1.16e-11 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 66.31 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 35 NHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSpfIE-RFNERIQDNngpisdaqlltlvqrleplvraqdv 113
Cdd:PRK00139 89 GHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGT--LGnGIGGELIPS------------------------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 114 ahpgfELTEFEIVTVlmFMYFEQMP---VDVVILEVgiggmwdSTQIIA----DKL---AAVITSVSYDHM--HvlgDTL 181
Cdd:PRK00139 142 -----GLTTPDALDL--QRLLAELVdagVTYAAMEV-------SSHALDqgrvDGLkfdVAVFTNLSRDHLdyH---GTM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 182 TEITQQKADIIAPGKP--VIVGDLP--QEALTVVQDIAQKR-DSDLYVYGQSFGMRTVDHQLTYvidqhklPVQLNLNGQ 256
Cdd:PRK00139 205 EDYLAAKARLFSELGLaaVINADDEvgRRLLALPDAYAVSMaGADLRATDVEYTDSGQTFTLVT-------EVESPLIGR 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917632672 257 YQIGNAAVAIktvqTVAPMLGVTIADAAIQ-EGLRHViwPARFETV--ADHPLVIVDGAHNVAGIDALVQTLR 326
Cdd:PRK00139 278 FNVSNLLAAL----AALLALGVPLEDALAAlAKLQGV--PGRMERVdaGQGPLVIVDYAHTPDALEKVLEALR 344
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
26-326 |
3.11e-11 |
|
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: 64.71 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 26 RLGFILATL-NHPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSpfIE-RFNERIQD--NNGPisDAqlLTLV 101
Cdd:COG0769 64 ALALLAAAFyGHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGT--VGnGIGGELIPssLTTP--EA--LDLQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 102 QRLEPLVRAQdvahpgfeltefeivtvlmfmyfeqmpVDVVILEVgiggmwdSTQIIA----DKL---AAVITSVSYDHM 174
Cdd:COG0769 138 RLLAEMVDAG---------------------------VTHVVMEV-------SSHALDqgrvDGVrfdVAVFTNLTRDHL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 175 --HvlgDTLTEITQQKA---DIIAPGKPVIV-----------GDLPQEALTVvqdiAQKRDSDLYV-------YGQSFGM 231
Cdd:COG0769 184 dyH---GTMEAYFAAKArlfDQLGPGGAAVInaddpygrrlaAAAPARVITY----GLKADADLRAtdielsaDGTRFTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 232 RTvdhqltyviDQHKLPVQLNLNGQYQIGNAAVAIktvqTVAPMLGVTIADaaIQEGLRHVIWPA-RFETV--ADHPLVI 308
Cdd:COG0769 257 VT---------PGGEVEVRLPLIGRFNVYNALAAI----AAALALGIDLEE--ILAALEKLKGVPgRMERVdgGQGPTVI 321
|
330
....*....|....*...
gi 917632672 309 VDGAHNVAGIDALVQTLR 326
Cdd:COG0769 322 VDYAHTPDALENVLEALR 339
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
294-365 |
1.85e-07 |
|
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: 48.49 E-value: 1.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917632672 294 WPARFE--TVADHPLVIVDGAHNVAGIDALVQTLRSSYGDKTVgIVFSALADK--HFEQMLRHLLAETNLKIVVVP 365
Cdd:pfam02875 1 VPGRLEvvGENNGVLVIDDYAHNPDAMEAALRALRNLFPGRLI-LVFGGMGDRdaEFHALLGRLAAALADVVILTG 75
|
|
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
164-338 |
2.05e-07 |
|
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: 52.76 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 164 AVITSVSYDHMHVLGDtLTEITQQ--K-ADIIAPGKPVIV-GDLPqealtVVQDIAQKRDSDLYVYGQSFG--MRTVDHQ 237
Cdd:COG0773 175 AVVTNIEADHLDIYGD-LEAIKEAfhEfARNVPFYGLLVLcADDP-----GLRELLPRCGRPVITYGFSEDadYRAENIR 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 238 LT--------YVIDQHKLPVQLNLNGQYQIGNAAVAIktvqTVAPMLGVTiaDAAIQEGL-------RhviwpaRFETVA 302
Cdd:COG0773 249 IDgggstfdvLRRGEELGEVELNLPGRHNVLNALAAI----AVALELGVD--PEAIAEALasfkgvkR------RFELKG 316
|
170 180 190
....*....|....*....|....*....|....*...
gi 917632672 303 DHP--LVIVDGAHNVAGIDALVQTLRSSYGDKTVGIVF 338
Cdd:COG0773 317 EVGgvTVIDDYAHHPTEIAATLAAAREKYPDRRLVAVF 354
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
46-266 |
2.20e-07 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 51.15 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 46 VTGTNGKGSTSQMMASILRAAnlqVGLFSSPFIeRFNERIQDNNGPISDAQLLTLVQRLEplvraqdvahpgfeltefei 125
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLA---GGVIGTIGT-YIGKSGNTTNNAIGLPLTLAEMVEAG-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 126 vtvlmfmyfeqmpVDVVILEVGIGGMwDSTQI--IADKLAAVITSVSYDHMHVLGdTLTEITQQKADIIA----PGKPVI 199
Cdd:pfam08245 57 -------------AEYAVLEVSSHGL-GEGRLsgLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEglpeDGIAVI 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917632672 200 VGDlpQEALTVVQDIAQKRDSDLYVYGQS--FGMRTVDHQLT---YVIDQHKLP-----VQLNLNGQYQIGNAAVAI 266
Cdd:pfam08245 122 NAD--DPYGAFLIAKLKKAGVRVITYGIEgeADLRAANIELSsdgTSFDLFTVPggeleIEIPLLGRHNVYNALAAI 196
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
36-326 |
4.69e-07 |
|
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: 52.01 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 36 HPEHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLFSSpFIERFNERIQDNNGPISDAQLLtlvQRLEPLVRAQDvah 115
Cdd:PRK11929 107 RPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGT-LGARLDGRLIPGSLTTPDAIIL---HRILARMRAAG--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 116 pgfeltefeivtvlmfmyfeqmpVDVVILEV-GIG---GMWDSTQIIadklAAVITSVSYDHMHVLGdTLTEITQQKADI 191
Cdd:PRK11929 180 -----------------------ADAVAMEAsSHGleqGRLDGLRIA----VAGFTNLTRDHLDYHG-TMQDYEEAKAAL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 192 IAPGKP----VIVGDLPQEALT------VVQDIAQKRDSDLYVYGQSFGMRTVDHQLTYVIDQHKLPVQLNLNGQYQIGN 261
Cdd:PRK11929 232 FSKLPGlgaaVINADDPAAARLlaalprGLKVGYSPQNAGADVQARDLRATAHGQVFTLATPDGSYQLVTRLLGRFNVSN 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917632672 262 AAVAIktvqtvAPMLGVTIADAAIQEGLRHVI-WPARFETVADH-----PLVIVDGAHNVAGIDALVQTLR 326
Cdd:PRK11929 312 LLLVA------AALKKLGLPLAQIARALAAVSpVPGRMERVGPTagaqgPLVVVDYAHTPDALAKALTALR 376
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
46-324 |
1.28e-06 |
|
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: 50.49 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 46 VTGTNGKGSTSQMMASILRAA----------NLQVGLfsspfierfneriqdnngpisdaqlltlvqrlePLvraqdvah 115
Cdd:COG0770 105 ITGSNGKTTTKEMLAAVLSTKgkvlatpgnfNNEIGV---------------------------------PL-------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 116 pgfeltefeivTVLmfmyfeQMPVD--VVILEVGI---GGMWDSTQIIA-DklAAVITSVSYDHMHVLGdTLTEITQQKA 189
Cdd:COG0770 144 -----------TLL------RLPEDheFAVLEMGMnhpGEIAYLARIARpD--IAVITNIGPAHLEGFG-SLEGIARAKG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 190 DIIA---PGKPVIV-GDLP------QEALTVVQDIAQKRDSDlyVYGQSFGMRTVDHQLTYVIDQHKLPVQLNLNGQYQI 259
Cdd:COG0770 204 EIFEglpPGGVAVLnADDPllaalaERAKARVLTFGLSEDAD--VRAEDIELDEDGTRFTLHTPGGELEVTLPLPGRHNV 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917632672 260 GNAAVAIktvqTVAPMLGVTIADaaIQEGLRHVIWPA-RFETV-ADHPLVIVDGAHN------VAGIDALVQT 324
Cdd:COG0770 282 SNALAAA----AVALALGLDLEE--IAAGLAAFQPVKgRLEVIeGAGGVTLIDDSYNanpdsmKAALDVLAQL 348
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
46-174 |
7.08e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 48.23 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 46 VTGTNGKGSTSQMMASILRAANLQVGLFSSP--FIErfNERIQ--DNNGPISDAQLLTlvqrleplvraqdvaHPGfelt 121
Cdd:PRK14016 485 VTGTNGKTTTTRLIAHILKLSGKRVGMTTTDgvYID--GRLIDkgDCTGPKSARRVLM---------------NPD---- 543
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 917632672 122 efeivtvlmfmyfeqmpVDVVILEVGIGGmwdstqIIADKLA------AVITSVSYDHM 174
Cdd:PRK14016 544 -----------------VEAAVLETARGG------ILREGLAydrcdvGVVTNIGEDHL 579
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
38-304 |
4.81e-04 |
|
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: 42.38 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 38 EHKQKYIHVTGTNGKGSTSQMMASILRAANLQVGLfsspfierfneriqdnNGPISDAqLLTLVQRLEPLvraqdvahpg 117
Cdd:COG0771 102 LSPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAV----------------GGNIGTP-LLDLLLEPEPP---------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 118 feltefeivtvlmfmyfeqmpvDVVILEVGiggmwdSTQII-ADKL---AAVITSVSYDHM--HvlgDTLTEITQQKADI 191
Cdd:COG0771 155 ----------------------DVYVLELS------SFQLEtTPSLrpdVAVILNITPDHLdrH---GSMEAYAAAKARI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632672 192 IAPGKP----VIVGDLPqealtVVQDIAQKRDSDLYVYG----QSFGMRTVDHQLTYVIDQHKL-PV-QLNLNGQYQIGN 261
Cdd:COG0771 204 FANQTPddyaVLNADDP-----LTRALAEEAKARVVPFSlkepLEGGAGLEDGKLVDRASGEELlPVdDLRLPGRHNLEN 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 917632672 262 AAVAIktvqTVAPMLGVtiADAAIQEGLR------HviwpaRFETVADH 304
Cdd:COG0771 279 ALAAL----AAARALGV--PPEAIREALRsfkglpH-----RLEFVAEI 316
|
|
| |
