|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10446 |
PRK10446 |
30S ribosomal protein S6--L-glutamate ligase; |
1-300 |
0e+00 |
|
30S ribosomal protein S6--L-glutamate ligase;
Pssm-ID: 182468 [Multi-domain] Cd Length: 300 Bit Score: 556.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 1 MKIAILSRDGSLYSCKRLREAAEDRGHSIDIIDPLSCYMNINPAAPTIHYRGRQLERYDAVIPRIGSAITFYGTAVLRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 161 ESVIDAFRGLNAHILVQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANTL 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 241 GLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYIEQRGRPGFRLKSGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-291 |
5.76e-113 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 328.05 E-value: 5.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 1 MKIAILSRDGSLYSCKRLREAAEDRGHSIDIIDPLSCYMNINPAAPtiHYRGRQLERYDAVIPRIGSaiTFYGTAVLRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 161 ESVIDAFRGL-NAHILVQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANT 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 727179689 240 LGLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYIEQRGR 291
Cdd:COG0189 237 LGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARAA 288
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
5.27e-110 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 320.06 E-value: 5.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 2 KIAILSRDGSLySCKRLREAAEDRGHSIDIIDPLSCYMNINPaaptihyRGRQLERYDAVIPRIgsAITFYGTAVLRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 82 LLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 162 SVIDAFRGLNA---HILVQEYVREAQGRDVRCLVVGGRVVAAIERQaKPGEFRSNLHRGGSARKVTITARERAIAVKAAN 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 727179689 239 TLGLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
97-286 |
5.12e-88 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 260.90 E-value: 5.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 97 ARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 176 VQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANTLGLDVAGVDILRAERG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 727179689 256 PLVMEVNASPGLEGVETTTGLDIAGMMIEYI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
3.75e-47 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 159.71 E-value: 3.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 2 KIAILSRDGSLYSCKRLREAAEDRGHSIDIIDPL----SCYMNINpaaptIHYRGRQLERYDAVIPRIGSAITFYGTA-- 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKDIDPVLIDLSkievSIGSDIK-----FKYGKINLLDLDAIFVRDIGAGSNEGVSfr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 76 --VLRQFELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGAplVVKLVEGTQGIGVVL 153
Cdd:NF040720 76 fdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGIVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 154 ---AETRQAAESVIDAFRGLNAHILVQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARER 230
Cdd:NF040720 154 iknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEEQE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 727179689 231 AIAVKAANTLGLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYIE 287
Cdd:NF040720 234 ELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 290
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10446 |
PRK10446 |
30S ribosomal protein S6--L-glutamate ligase; |
1-300 |
0e+00 |
|
30S ribosomal protein S6--L-glutamate ligase;
Pssm-ID: 182468 [Multi-domain] Cd Length: 300 Bit Score: 556.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 1 MKIAILSRDGSLYSCKRLREAAEDRGHSIDIIDPLSCYMNINPAAPTIHYRGRQLERYDAVIPRIGSAITFYGTAVLRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 161 ESVIDAFRGLNAHILVQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANTL 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 241 GLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYIEQRGRPGFRLKSGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-291 |
5.76e-113 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 328.05 E-value: 5.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 1 MKIAILSRDGSLYSCKRLREAAEDRGHSIDIIDPLSCYMNINPAAPtiHYRGRQLERYDAVIPRIGSaiTFYGTAVLRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 161 ESVIDAFRGL-NAHILVQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANT 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 727179689 240 LGLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYIEQRGR 291
Cdd:COG0189 237 LGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARAA 288
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
5.27e-110 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 320.06 E-value: 5.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 2 KIAILSRDGSLySCKRLREAAEDRGHSIDIIDPLSCYMNINPaaptihyRGRQLERYDAVIPRIgsAITFYGTAVLRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 82 LLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 162 SVIDAFRGLNA---HILVQEYVREAQGRDVRCLVVGGRVVAAIERQaKPGEFRSNLHRGGSARKVTITARERAIAVKAAN 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 727179689 239 TLGLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
97-286 |
5.12e-88 |
|
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.
Pssm-ID: 369879 [Multi-domain] Cd Length: 188 Bit Score: 260.90 E-value: 5.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 97 ARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 176 VQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANTLGLDVAGVDILRAERG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 727179689 256 PLVMEVNASPGLEGVETTTGLDIAGMMIEYI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
|
|
| Rimk_N |
pfam18030 |
RimK PreATP-grasp domain; This is the N-terminal domain found in Escherichia coli RimK ... |
1-94 |
1.43e-58 |
|
RimK PreATP-grasp domain; This is the N-terminal domain found in Escherichia coli RimK proteins (Ribosomal protein S6-L-glutamate ligase). This domain precedes the ATP-grasp domain pfam08443.
Pssm-ID: 465621 [Multi-domain] Cd Length: 94 Bit Score: 182.28 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 1 MKIAILSRDGSLYSCKRLREAAEDRGHSIDIIDPLSCYMNINPAAPTIHYRGRQLERYDAVIPRIGSAITFYGTAVLRQF 80
Cdd:pfam18030 1 MKIAILSRNPNLYSTRRLVEAAEARGHEVEVIDPLRCYMNIESGKPEIHYKGEPLPDFDAVIPRIGASITFYGTAVLRQF 80
|
90
....*....|....
gi 727179689 81 ELLGSYPLNESVAI 94
Cdd:pfam18030 81 EMMGVFSLNSSQAI 94
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
3.75e-47 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 159.71 E-value: 3.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 2 KIAILSRDGSLYSCKRLREAAEDRGHSIDIIDPL----SCYMNINpaaptIHYRGRQLERYDAVIPRIGSAITFYGTA-- 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKDIDPVLIDLSkievSIGSDIK-----FKYGKINLLDLDAIFVRDIGAGSNEGVSfr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 76 --VLRQFELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGAplVVKLVEGTQGIGVVL 153
Cdd:NF040720 76 fdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGIVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 154 ---AETRQAAESVIDAFRGLNAHILVQEYVREAQGRDVRCLVVGGRVVAAIERQAKPGEFRSNLHRGGSARKVTITARER 230
Cdd:NF040720 154 iknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEEQE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 727179689 231 AIAVKAANTLGLDVAGVDILRAERGPLVMEVNASPGLEGVETTTGLDIAGMMIEYIE 287
Cdd:NF040720 234 ELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 290
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
91-267 |
5.37e-19 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 87.13 E-value: 5.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 91 SVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGaPLVVKLVEGTQGIGVVL-AETRQAAESVIDAFRG 169
Cdd:PRK14016 206 AIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGY-PVVVKPLDGNHGRGVTVnITTREEIEAAYAVASK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 170 LNAHILVQEYVReaqGRDVRCLVVGGRVVAAIER-----------------------------QAKP------------- 207
Cdd:PRK14016 285 ESSDVIVERYIP---GKDHRLLVVGGKLVAAARRepphvigdgkhtirelieivnqdprrgegHEKPltkiklddialle 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 208 --------------GE---FRS--NLHRGGSARKVT--ITARERAIAVKAANTLGLDVAGVD-----ILR--AERGPLVM 259
Cdd:PRK14016 362 lakqgytldsvppkGEkvyLRRnaNLSTGGTAIDVTdeVHPENAAIAERAAKIIGLDIAGVDvvcedISKplEEQGGAIV 441
|
....*...
gi 727179689 260 EVNASPGL 267
Cdd:PRK14016 442 EVNAAPGL 449
|
|
| PRK05246 |
PRK05246 |
glutathione synthetase; Provisional |
174-289 |
2.51e-18 |
|
glutathione synthetase; Provisional
Pssm-ID: 235371 [Multi-domain] Cd Length: 316 Bit Score: 83.22 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 174 ILVQEYVREAQGRDVRCLVVGGRVV-AAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANTL---GLDVAGVDI 249
Cdd:PRK05246 195 VMAQRYLPEIKEGDKRILLVDGEPVgYALARIPAGGETRGNLAAGGRGEATPLTERDREICAAIGPELkerGLIFVGIDV 274
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 727179689 250 LraerGPLVMEVN-ASP-GLEGVETTTGLDIAGMMIEYIEQR 289
Cdd:PRK05246 275 I----GDYLTEINvTSPtGIREIERLTGVDIAGMLWDAIEAK 312
|
|
| PRK12458 |
PRK12458 |
glutathione synthetase; Provisional |
115-288 |
2.27e-17 |
|
glutathione synthetase; Provisional
Pssm-ID: 183536 [Multi-domain] Cd Length: 338 Bit Score: 80.84 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 115 PITGFAHSPDDTGDLIELVGGAPLVVKLVEGTQGIGVVLAET--RQAAESVIDAFRGLNaHILVQEYVREAQGRDVRCLV 192
Cdd:PRK12458 142 PTTHISRNKEYIREFLEESPGDKMILKPLQGSGGQGVFLIEKsaQSNLNQILEFYSGDG-YVIAQEYLPGAEEGDVRILL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 193 VGGR------VVAAIERQAKPGEFRSNLHRGGSARKVTITARERAIAVKAANTL---GLDVAGVDILraerGPLVMEVNA 263
Cdd:PRK12458 221 LNGEplerdgHYAAMRRVPAGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPKLvrdGLFFVGLDIV----GDKLVEVNV 296
|
170 180
....*....|....*....|....*..
gi 727179689 264 -SP-GLEGVETTTGLDIAGMMIEYIEQ 288
Cdd:PRK12458 297 fSPgGLTRINKLNKIDFVEDIIEALER 323
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
59-283 |
5.03e-15 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 73.37 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 59 DAVIPriGSAITFYGTAVLRqfELLGsYPLNESVAITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGaPL 138
Cdd:COG0439 19 DAVLS--ESEFAVETAAELA--EELG-LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGY-PV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 139 VVKLVEGTQGIGVVLAETRQAAESVIDAFRG------LNAHILVQEYVreaQGRD--VRCLVVGGRVV--AAIERQAKPG 208
Cdd:COG0439 93 VVKPADGAGSRGVRVVRDEEELEAALAEARAeakagsPNGEVLVEEFL---EGREysVEGLVRDGEVVvcSITRKHQKPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 209 EFRSNLHRGGSARKVTITARERAIAVKAANTLGLD--VAGVDILRAERG-PLVMEVNASPGLEG----VETTTGLDIAGM 281
Cdd:COG0439 170 YFVELGHEAPSPLPEELRAEIGELVARALRALGYRrgAFHTEFLLTPDGePYLIEINARLGGEHipplTELATGVDLVRE 249
|
..
gi 727179689 282 MI 283
Cdd:COG0439 250 QI 251
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
1-267 |
3.43e-14 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 71.29 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 1 MKIAILS------RDGSLYSCKRLREAAEDRGHS-----IDIIDPLSCYMNINPAA--PTIHyrGRQLEryDAVIPRIgs 67
Cdd:COG1181 1 MRVAVLFggrsaeREVSLKSGRAVAAALDKAGYDvvpigIDVEDLPAALKELKPDVvfPALH--GRGGE--DGTIQGL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 68 aitfygtavlrqFELL-----GSYPLNESVAItrarDKLRSLQLLARQGIdlPITGFAH-SPDDTGDLIELVG--GAPLV 139
Cdd:COG1181 75 ------------LELLgipytGSGVLASALAM----DKALTKRVLAAAGL--PTPPYVVlRRGELADLEAIEEelGLPLF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 140 VKLV-EGTqGIGVVLAETRQAAESVIDAFRGLNAHILVQEYVReaqGRDVRCLVVGGRVVAA---IERQAKpGEFRSNLH 215
Cdd:COG1181 137 VKPArEGS-SVGVSKVKNAEELAAALEEAFKYDDKVLVEEFID---GREVTVGVLGNGGPRAlppIEIVPE-NGFYDYEA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727179689 216 R--GGSARKVT-------ITARERAIAVKAANTLGL-DVAGVD-ILRAERGPLVMEVNASPGL 267
Cdd:COG1181 212 KytDGGTEYICparlpeeLEERIQELALKAFRALGCrGYARVDfRLDEDGEPYLLEVNTLPGM 274
|
|
| GSH-S_ATP |
pfam02955 |
Prokaryotic glutathione synthetase, ATP-grasp domain; |
139-266 |
9.77e-14 |
|
Prokaryotic glutathione synthetase, ATP-grasp domain;
Pssm-ID: 427078 [Multi-domain] Cd Length: 175 Bit Score: 67.97 E-value: 9.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 139 VVKLVEGTQGIGVV-LAETRQAAESVIDAFRGL-NAHILVQEYVREAQGRDVRCLVVGGRVV-AAIERQAKPGEFRSNLH 215
Cdd:pfam02955 35 ILKPLDGMGGAGIFrVKKGDPNLNVILETLTQYgTRPVMAQRYLPEIKEGDKRILLINGEPIgYALARIPAAGEFRGNLA 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 727179689 216 RGGSARKVTITARERAIAVKAANTL---GLDVAGVDILraerGPLVMEVN-ASPG 266
Cdd:pfam02955 115 AGGRGEATPLTERDREICETIGPKLkerGLFFVGLDVI----GDYLTEINvTSPT 165
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
99-267 |
1.50e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 54.73 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 99 DKLRSLQLLarQGIDLPITGFAH-SPDDTGDLIELVGGAPLVVKLVEGTQGIGVVLAETRQA-AESVIDAFRgLNAHILV 176
Cdd:PRK01372 98 DKLRTKLVW--QAAGLPTPPWIVlTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDElQAALELAFK-YDDEVLV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 177 QEYVreaQGRDVRCLVVGGRVVAAIERQAkPGEF---RSNLHRGGSARKV------TITARERAIAVKAANTLGLDVAG- 246
Cdd:PRK01372 175 EKYI---KGRELTVAVLGGKALPVIEIVP-AGEFydyEAKYLAGGTQYICpaglpaEIEAELQELALKAYRALGCRGWGr 250
|
170 180
....*....|....*....|..
gi 727179689 247 VD-ILRAERGPLVMEVNASPGL 267
Cdd:PRK01372 251 VDfMLDEDGKPYLLEVNTQPGM 272
|
|
| MfnD |
COG1821 |
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme ... |
53-284 |
3.26e-08 |
|
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme transport and metabolism];
Pssm-ID: 441426 [Multi-domain] Cd Length: 323 Bit Score: 53.78 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 53 RQLERYDAVIP----------RIGSAITFYGTAvlrqfeLLGSYPlnESVAItrARDKLRSLQLLARQGIDLPITGFAhs 122
Cdd:COG1821 78 RLAAEADAVLViapetdgilaRLTRIVEAAGKR------NLGSSP--EAIAL--AADKLLTAELLAAAGIPTPPTFPA-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 123 pddtGDLIELVGGaPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLnahiLVQEYVrEAQGRDVRCLVVGGRV-VAAI 201
Cdd:COG1821 146 ----DDAPPLLAG-PWVVKPDDGAGSEGTRLFDDPAALRAREARGAGL----IVQPYI-EGEAASLSLLCGRGGAlLLSI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 202 ERQA---KPGEFRsnlHRGGsarKV----TITARERAIAVKAANTL----GLdvAGVDILRAERGPLVMEVNASPglegv 270
Cdd:COG1821 216 NRQRievDGGRFS---YLGG---TVpaehPRKEELQALAQKVAEALpglrGY--VGVDLILTADGPVVVEVNPRL----- 282
|
250 260
....*....|....*....|..
gi 727179689 271 eTT--------TGLDIAGMMIE 284
Cdd:COG1821 283 -TTsyvglraaLGENLAALLLD 303
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
97-266 |
2.37e-07 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 49.69 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 97 ARDKLRSLQLLARQGIDLPITGFAHSPDDTGDlielvggaPLVVKLVEGTQGIGVVLAETRQAAESVIDafrglnaHILV 176
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQAEELLREEK--------KYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 177 QEYVrEAQGRDVRCLVVGGRV-VAAIERQAKPGEFRSNLHRGGSARKVTITARE-RAIAVKAA----NTLGLdvAGVDIL 250
Cdd:pfam02655 66 QEFI-EGEPLSVSLLSDGEKAlPLSVNRQYIDNGGSGFVYAGNVTPSRTELKEEiIELAEEVVeclpGLRGY--VGVDLV 142
|
170
....*....|....*.
gi 727179689 251 RAERGPLVMEVNASPG 266
Cdd:pfam02655 143 LKDNEPYVIEVNPRIT 158
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
93-294 |
1.09e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.85 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 93 AITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLieLVGGA-PLVVKLVEGTQGIGVVLAETRQAA-ESVIDAFRGL 170
Cdd:PRK02186 101 AIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDA--LDGLTyPVVVKPRMGSGSVGVRLCASVAEAaAHCAALRRAG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 171 NAHILVQEYVREAQGRDVRCLVVGGRVVAAIERQ--AKPGEFRSNLHRGGSARKVTITARERAIAVKAANTLGLDV--AG 246
Cdd:PRK02186 179 TRAALVQAYVEGDEYSVETLTVARGHQVLGITRKhlGPPPHFVEIGHDFPAPLSAPQRERIVRTVLRALDAVGYAFgpAH 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 727179689 247 VDILRAERGPLVMEVNasPGLEG------VETTTGLDIAGMMIEYieQRGRPGF 294
Cdd:PRK02186 259 TELRVRGDTVVIIEIN--PRLAGgmipvlLEEAFGVDLLDHVIDL--HLGVAAF 308
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
94-263 |
1.50e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 48.73 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 94 ITRARDKLRSLQLLARQGIDLPITgfaHSPDDTGDLIELVGGA----PLVVKLVEGTQGIGVVLAETRQAAESVIDafrg 169
Cdd:PRK12767 106 IEICNDKWLTYEFLKENGIPTPKS---YLPESLEDFKAALAKGelqfPLFVKPRDGSASIGVFKVNDKEELEFLLE---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 170 LNAHILVQEYVREAQ-GRDVRCLvVGGRVVAAIERqaKPGEFRSnlhrGGSARKVTITARE-RAIAVKAANTLG----LD 243
Cdd:PRK12767 179 YVPNLIIQEFIEGQEyTVDVLCD-LNGEVISIVPR--KRIEVRA----GETSKGVTVKDPElFKLAERLAEALGargpLN 251
|
170 180
....*....|....*....|
gi 727179689 244 vagVDILRAERGPLVMEVNA 263
Cdd:PRK12767 252 ---IQCFVTDGEPYLFEINP 268
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
93-266 |
2.93e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 48.00 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 93 AITRARDKLRSLQLLARQGIDLPITGFAHSPDDTGDLIELVGGaPLVVK--------LVEGTQGIGVVLAETRQAAESVI 164
Cdd:COG3919 111 LLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF-PVVVKpadsvgydELSFPGKKKVFYVDDREELLALL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 165 DAFRGLNAHILVQEYV--REAQGRDVRCLV-VGGRVVAA----IERQAKPgefrsnlHRGGSArkVTITARERAIAVKAA 237
Cdd:COG3919 190 RRIAAAGYELIVQEYIpgDDGEMRGLTAYVdRDGEVVATftgrKLRHYPP-------AGGNSA--ARESVDDPELEEAAR 260
|
170 180 190
....*....|....*....|....*....|....*
gi 727179689 238 NTLG-LD---VAGVDILRAERG--PLVMEVNASPG 266
Cdd:COG3919 261 RLLEaLGyhgFANVEFKRDPRDgeYKLIEINPRFW 295
|
|
| ATPgrasp_YheCD |
pfam14398 |
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ... |
138-285 |
8.01e-06 |
|
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the modification/biosynthesis of spore-wall and capsular proteins.
Pssm-ID: 405146 [Multi-domain] Cd Length: 256 Bit Score: 46.40 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 138 LVVKLVEGTQGIGVVLAE------------TRQAAESVIDAFRGLNAHI---------LVQEYVR--EAQGR--DVRCLV 192
Cdd:pfam14398 51 VYLKPVNGSLGKGILRIEkdgggyylygryGKNSKTNRFLDFSELESFLrrllgkkryIIQQGIDlaTIDGRpfDFRVLV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 193 V-GGR----VVAAIERQAKPGEFRSNLHRGGSA--------------RKVTITARERAIAVKAANT----------LGLD 243
Cdd:pfam14398 131 QkNGKgkwvVTGIAARIAGPGSITTNLSGGGTAipleealrrafgeeRAEKILEKLEELALELARAleesfgglgeLGLD 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 727179689 244 VaGVDilraERGPLVM-EVNASPG----LEGVETTTGLDIAGMMIEY 285
Cdd:pfam14398 211 L-GID----KNGRVWLlEVNSKPGrsifTHAGDKELIRKSVKRPLEY 252
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
78-284 |
3.07e-05 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 44.91 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 78 RQFELLGsyplNESVAITRARDKLRSLQLLARQGIDLPITGFAhSPDDTGdlielvggaPLVVKLVEGTQGIGVVLAETR 157
Cdd:COG2232 95 RRLPLLG----NPPEVVRRVKDPLRFFALLDELGIPHPETRFE-PPPDPG---------PWLVKPIGGAGGWHIRPADSE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 158 QAAEsvidafrglnAHILVQEYVreaQGRDVRCLVV--GGRVVA-AIERQAKPGEFRSNLHRGGSARKVTITARERAIAV 234
Cdd:COG2232 161 APPA----------PGRYFQRYV---EGTPASVLFLadGSDARVlGFNRQLIGPAGERPFRYGGNIGPLALPPALAEEMR 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 727179689 235 KAANTL-------GLdvAGVDILRAERGPLVMEVNASPG--LEGVETTTGLDIAGMMIE 284
Cdd:COG2232 228 AIAEALvaalglvGL--NGVDFILDGDGPYVLEVNPRPQasLDLYEDATGGNLFDAHLR 284
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
118-266 |
4.01e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 43.84 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 118 GFAHSPDDTGDLIELVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYVReaqGRDVRCLVVG--- 194
Cdd:pfam07478 19 DWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIE---GREIECAVLGned 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 195 GRVVAAIERQAKPGEFRSNLHRGGSARKVTITA--------RERAIAVKAANTLGL-DVAGVDI-LRAERGPLVMEVNAS 264
Cdd:pfam07478 96 PEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPAdleeeqeeQIQELALKAYKALGCrGLARVDFfLTEDGEIVLNEVNTI 175
|
..
gi 727179689 265 PG 266
Cdd:pfam07478 176 PG 177
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
97-269 |
3.50e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 41.81 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 97 ARDKLRSLQLLARQGI------DLPITGFAHSPDDTgdLIELVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRG 169
Cdd:PRK14572 128 AMDKTRANQIFLQSGQkvapffELEKLKYLNSPRKT--LLKLESlGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 170 LNAHILVQEYVreaQGRDVRCLVV----GGRV--VAAIERQAKPG----EFRSNLHRGGSaRKVT-------ITARERAI 232
Cdd:PRK14572 206 SDSKVMSQSFL---SGTEVSCGVLeryrGGKRnpIALPATEIVPGgeffDFESKYKQGGS-EEITparisdqEMKRVQEL 281
|
170 180 190
....*....|....*....|....*....|....*...
gi 727179689 233 AVKAANTLGLD-VAGVDILRAERGPLVMEVNASPGLEG 269
Cdd:PRK14572 282 AIRAHESLGCKgYSRTDFIIVDGEPHILETNTLPGMTE 319
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
175-265 |
7.60e-03 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 36.05 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179689 175 LVQEYVrEAQGRDVRCLVVGGRVVAAIERqakpgefrsnlhRGGSARKVTITARERAI--AVKAANTLGLD-VAGVDILR 251
Cdd:pfam15632 6 LVMEYL-PGPEYSVDCLAGHGELIAAVPR------------RKGDGGIQTLEDDPELIeaARRLAEAFGLDgLFNVQFRY 72
|
90
....*....|....
gi 727179689 252 AERGPLVMEVNASP 265
Cdd:pfam15632 73 DGDGPKLLEINPRM 86
|
|
| |
