|
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: 600.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 1 MKIAILSRDGTLYSCKRLREAAMKRGHLVEILDPLSCYMNISPAASSIHYKGRQLPHFDAVIPRIGSAITFYGTAALRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 81 EMLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 161 ESVIDAFRGLNAHILVQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQTM 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 241 GLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWIERHATPEFCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
3.38e-117 |
|
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: 338.17 E-value: 3.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 2 KIAILSRDGTLySCKRLREAAMKRGHLVEILDPLSCYMNISPaassihyKGRQLPHFDAVIPRIgsAITFYGTAALRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 82 MLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 162 SVIDAFRGLNA---HILVQEYIKEARGRDIRCLVVGDEVVAAIERRaKEGDFRSNLHRGGMASIASITPREREIAIKAAQ 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 581978245 239 TMGLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-290 |
5.29e-112 |
|
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: 325.36 E-value: 5.29e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 1 MKIAILSRDGTLYSCKRLREAAMKRGHLVEILDPLSCYMNISPAASsiHYKGRQLPHFDAVIPRIGSaiTFYGTAALRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 81 EMLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 161 ESVIDAFRGL-NAHILVQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQT 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 581978245 240 MGLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWIERHA 290
Cdd:COG0189 237 LGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARA 287
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
97-286 |
4.96e-99 |
|
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: 288.63 E-value: 4.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 97 ARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 176 VQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQTMGLDVAGVDILRAERG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 581978245 256 PLVMEVNASPGLEGVEKTTGVDIAGRMIQWI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
1.80e-50 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 168.18 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 2 KIAILSRDGTLYSCKRLREAAMKRGhlveiLDPLscYMNISPAASSIH------YKGRQLPHFDAVIPRIGSAITFYGTA 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 76 ----ALRQFEMLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720 74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPR 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 581978245 229 EREIAIKAAQTMGLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWIE 287
Cdd:NF040720 232 QEELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 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: 600.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 1 MKIAILSRDGTLYSCKRLREAAMKRGHLVEILDPLSCYMNISPAASSIHYKGRQLPHFDAVIPRIGSAITFYGTAALRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 81 EMLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 161 ESVIDAFRGLNAHILVQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQTM 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 241 GLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWIERHATPEFCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
3.38e-117 |
|
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: 338.17 E-value: 3.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 2 KIAILSRDGTLySCKRLREAAMKRGHLVEILDPLSCYMNISPaassihyKGRQLPHFDAVIPRIgsAITFYGTAALRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 82 MLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 162 SVIDAFRGLNA---HILVQEYIKEARGRDIRCLVVGDEVVAAIERRaKEGDFRSNLHRGGMASIASITPREREIAIKAAQ 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 581978245 239 TMGLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-290 |
5.29e-112 |
|
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: 325.36 E-value: 5.29e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 1 MKIAILSRDGTLYSCKRLREAAMKRGHLVEILDPLSCYMNISPAASsiHYKGRQLPHFDAVIPRIGSaiTFYGTAALRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 81 EMLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 161 ESVIDAFRGL-NAHILVQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQT 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 581978245 240 MGLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWIERHA 290
Cdd:COG0189 237 LGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARA 287
|
|
| RimK |
pfam08443 |
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ... |
97-286 |
4.96e-99 |
|
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: 288.63 E-value: 4.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 97 ARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 176 VQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQTMGLDVAGVDILRAERG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 581978245 256 PLVMEVNASPGLEGVEKTTGVDIAGRMIQWI 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 |
2.52e-56 |
|
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: 176.51 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 1 MKIAILSRDGTLYSCKRLREAAMKRGHLVEILDPLSCYMNISPAASSIHYKGRQLPHFDAVIPRIGSAITFYGTAALRQF 80
Cdd:pfam18030 1 MKIAILSRNPNLYSTRRLVEAAEARGHEVEVIDPLRCYMNIESGKPEIHYKGEPLPDFDAVIPRIGASITFYGTAVLRQF 80
|
90
....*....|....
gi 581978245 81 EMLGSYPLNESVAI 94
Cdd:pfam18030 81 EMMGVFSLNSSQAI 94
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
1.80e-50 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 168.18 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 2 KIAILSRDGTLYSCKRLREAAMKRGhlveiLDPLscYMNISPAASSIH------YKGRQLPHFDAVIPRIGSAITFYGTA 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 76 ----ALRQFEMLGSYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720 74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIKEARGRDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGMASIASITPR 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 581978245 229 EREIAIKAAQTMGLDVAGVDILRAERGPLVMEVNASPGLEGVEKTTGVDIAGRMIQWIE 287
Cdd:NF040720 232 QEELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 290
|
|
| PRK12458 |
PRK12458 |
glutathione synthetase; Provisional |
115-288 |
9.26e-20 |
|
glutathione synthetase; Provisional
Pssm-ID: 183536 [Multi-domain] Cd Length: 338 Bit Score: 87.77 E-value: 9.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 115 PVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAET--RQAAESVIDAFRGLNaHILVQEYIKEARGRDIRCLV 192
Cdd:PRK12458 142 PTTHISRNKEYIREFLEESPGDKMILKPLQGSGGQGVFLIEKsaQSNLNQILEFYSGDG-YVIAQEYLPGAEEGDVRILL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 193 V------GDEVVAAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQTM---GLDVAGVDILraerGPLVMEVNA 263
Cdd:PRK12458 221 LngepleRDGHYAAMRRVPAGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPKLvrdGLFFVGLDIV----GDKLVEVNV 296
|
170 180
....*....|....*....|....*..
gi 581978245 264 -SP-GLEGVEKTTGVDIAGRMIQWIER 288
Cdd:PRK12458 297 fSPgGLTRINKLNKIDFVEDIIEALER 323
|
|
| PRK05246 |
PRK05246 |
glutathione synthetase; Provisional |
174-288 |
2.25e-19 |
|
glutathione synthetase; Provisional
Pssm-ID: 235371 [Multi-domain] Cd Length: 316 Bit Score: 86.30 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 174 ILVQEYIKEARGRDIRCLVVGDEVV-AAIERRAKEGDFRSNLHRGGMASIASITPREREIAIKAAQTM---GLDVAGVDI 249
Cdd:PRK05246 195 VMAQRYLPEIKEGDKRILLVDGEPVgYALARIPAGGETRGNLAAGGRGEATPLTERDREICAAIGPELkerGLIFVGIDV 274
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 581978245 250 LraerGPLVMEVN-ASP-GLEGVEKTTGVDIAGRMIQWIER 288
Cdd:PRK05246 275 I----GDYLTEINvTSPtGIREIERLTGVDIAGMLWDAIEA 311
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
91-267 |
2.00e-18 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 85.21 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 91 SVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVL-AETRQAAESVIDAFRG 169
Cdd:PRK14016 206 AIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGY-PVVVKPLDGNHGRGVTVnITTREEIEAAYAVASK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 170 LNAHILVQEYIkeaRGRDIRCLVVGDEVVAAIERRAKE--GDFRSNLH-----------RG------------------- 217
Cdd:PRK14016 285 ESSDVIVERYI---PGKDHRLLVVGGKLVAAARREPPHviGDGKHTIRelieivnqdprRGeghekpltkiklddialle 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 218 ----GMaSIASITPRER----------------------------EIAIKAAQTMGLDVAGVD-----ILR--AERGPLV 258
Cdd:PRK14016 362 lakqGY-TLDSVPPKGEkvylrrnanlstggtaidvtdevhpenaAIAERAAKIIGLDIAGVDvvcedISKplEEQGGAI 440
|
....*....
gi 581978245 259 MEVNASPGL 267
Cdd:PRK14016 441 VEVNAAPGL 449
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
58-284 |
8.05e-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: 72.60 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 58 FDAVIPriGSAITFYGTAALRqfEMLGsYPLNESVAITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaP 137
Cdd:COG0439 18 IDAVLS--ESEFAVETAAELA--EELG-LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGY-P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 138 LVVKLVEGTQGIGVVLAETRQAAESVIDAFRG------LNAHILVQEYIkeaRGRDIRCLVVGDE---VVAAIERRAKEG 208
Cdd:COG0439 92 VVVKPADGAGSRGVRVVRDEEELEAALAEARAeakagsPNGEVLVEEFL---EGREYSVEGLVRDgevVVCSITRKHQKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 209 DFRsnLHRGGMASiASITPRER----EIAIKAAQTMGLD--VAGVDILRAERG-PLVMEVNASPGLEG----VEKTTGVD 277
Cdd:COG0439 169 PYF--VELGHEAP-SPLPEELRaeigELVARALRALGYRrgAFHTEFLLTPDGePYLIEINARLGGEHipplTELATGVD 245
|
....*..
gi 581978245 278 IAGRMIQ 284
Cdd:COG0439 246 LVREQIR 252
|
|
| GSH-S_ATP |
pfam02955 |
Prokaryotic glutathione synthetase, ATP-grasp domain; |
139-275 |
1.79e-14 |
|
Prokaryotic glutathione synthetase, ATP-grasp domain;
Pssm-ID: 427078 [Multi-domain] Cd Length: 175 Bit Score: 69.90 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 139 VVKLVEGTQGIGVV-LAETRQAAESVIDAFRGL-NAHILVQEYIKEARGRDIRCLVVGDEVV-AAIERRAKEGDFRSNLH 215
Cdd:pfam02955 35 ILKPLDGMGGAGIFrVKKGDPNLNVILETLTQYgTRPVMAQRYLPEIKEGDKRILLINGEPIgYALARIPAAGEFRGNLA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581978245 216 RGGMASIASITPREREIAIKAAQTM---GLDVAGVDILraerGPLVMEVN-ASP-GLEGVEKTTG 275
Cdd:pfam02955 115 AGGRGEATPLTERDREICETIGPKLkerGLFFVGLDVI----GDYLTEINvTSPtGIREIERLTG 175
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
97-267 |
1.98e-13 |
|
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: 69.36 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 97 ARDKLRSLQLLARQGIDLPvTGIAHSPDDTSDLIDMVG--GAPLVVKLV-EGTqGIGVVLAETRQAAESVIDAFRGLNAH 173
Cdd:COG1181 93 AMDKALTKRVLAAAGLPTP-PYVVLRRGELADLEAIEEelGLPLFVKPArEGS-SVGVSKVKNAEELAAALEEAFKYDDK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 174 ILVQEYIKearGRDIRCLVVGDEVVAA---IERRAKEG--DFRSNLHRGGMASI--ASITPRE----REIAIKAAQTMGL 242
Cdd:COG1181 171 VLVEEFID---GREVTVGVLGNGGPRAlppIEIVPENGfyDYEAKYTDGGTEYIcpARLPEELeeriQELALKAFRALGC 247
|
170 180
....*....|....*....|....*..
gi 581978245 243 -DVAGVD-ILRAERGPLVMEVNASPGL 267
Cdd:COG1181 248 rGYARVDfRLDEDGEPYLLEVNTLPGM 274
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
99-267 |
4.19e-11 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 62.44 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 99 DKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQA-AESVIDAFRgLNAHILVQ 177
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLG-LPLVVKPAREGSSVGVSKVKEEDElQAALELAFK-YDDEVLVE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 178 EYIKearGRDIRCLVVGDEVVAAIERRAKEG--DFRSNLHRGGMASI------ASITPREREIAIKAAQTMGLDVAG-VD 248
Cdd:PRK01372 176 KYIK---GRELTVAVLGGKALPVIEIVPAGEfyDYEAKYLAGGTQYIcpaglpAEIEAELQELALKAYRALGCRGWGrVD 252
|
170 180
....*....|....*....|
gi 581978245 249 -ILRAERGPLVMEVNASPGL 267
Cdd:PRK01372 253 fMLDEDGKPYLLEVNTQPGM 272
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
97-266 |
5.80e-08 |
|
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: 51.23 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 97 ARDKLRSLQLLARQGIDLPVTGIAHSPDdtsdlidmVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDafrglnaHILV 176
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQAEELL--------REEKKYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 177 QEYIKE--------ARGRDIRCLVVGDEVVAAierraKEGDFRsnlHRGGMA-SIASITPREREIAIKAAQTM-GL-DVA 245
Cdd:pfam02655 66 QEFIEGeplsvsllSDGEKALPLSVNRQYIDN-----GGSGFV---YAGNVTpSRTELKEEIIELAEEVVECLpGLrGYV 137
|
170 180
....*....|....*....|.
gi 581978245 246 GVDILRAERGPLVMEVNASPG 266
Cdd:pfam02655 138 GVDLVLKDNEPYVIEVNPRIT 158
|
|
| MfnD |
COG1821 |
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme ... |
83-284 |
9.41e-08 |
|
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme transport and metabolism];
Pssm-ID: 441426 [Multi-domain] Cd Length: 323 Bit Score: 52.62 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 83 LGSYPlnESVAItrARDKLRSLQLLARQGIDLPVTgiaHSPDDTSDLidmvGGAPLVVKLVEGTQGIGVVLAETRQAAES 162
Cdd:COG1821 112 LGSSP--EAIAL--AADKLLTAELLAAAGIPTPPT---FPADDAPPL----LAGPWVVKPDDGAGSEGTRLFDDPAALRA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 163 VIDAFRGLnahiLVQEYIK-EA-------RGRDIRCLVVGDEvvaAIERRakEGDFRsnLHRGGMASIASITPREREIAI 234
Cdd:COG1821 181 REARGAGL----IVQPYIEgEAaslsllcGRGGALLLSINRQ---RIEVD--GGRFS--YLGGTVPAEHPRKEELQALAQ 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 581978245 235 KAAQTM----GLdvAGVDILRAERGPLVMEVNASP--GLEGVEKTTGVDIAGRMIQ 284
Cdd:COG1821 250 KVAEALpglrGY--VGVDLILTADGPVVVEVNPRLttSYVGLRAALGENLAALLLD 303
|
|
| ATPgrasp_YheCD |
pfam14398 |
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ... |
124-266 |
1.18e-07 |
|
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: 51.80 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 124 DDTSDLIDMVGGAPLV-VKLVEGTQGIGVVLAE------------TRQAAESVIDAFRGLNAHI---------LVQEYIK 181
Cdd:pfam14398 36 QSPEDLERMLEKYGSVyLKPVNGSLGKGILRIEkdgggyylygryGKNSKTNRFLDFSELESFLrrllgkkryIIQQGID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 182 --EARGR--DIRCLVVGDE-----VVAAIERRAKEGDFRSNLHRGGMAS--------------IASITPREREIAIKAAQ 238
Cdd:pfam14398 116 laTIDGRpfDFRVLVQKNGkgkwvVTGIAARIAGPGSITTNLSGGGTAIpleealrrafgeerAEKILEKLEELALELAR 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 581978245 239 T----------MGLDVaGVDilraERGPLVM-EVNASPG 266
Cdd:pfam14398 196 AleesfgglgeLGLDL-GID----KNGRVWLlEVNSKPG 229
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
135-266 |
1.80e-07 |
|
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: 50.78 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 135 GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIkeaRGRDIRCLVVGDE--VVAAIERRAKEGDF-- 210
Cdd:pfam07478 36 GYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGI---EGREIECAVLGNEdpEVSPVGEIVPSGGFyd 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581978245 211 --RSNLHRGGMASIASITPRE-----REIAIKAAQTMGL-DVAGVDI-LRAERGPLVMEVNASPG 266
Cdd:pfam07478 113 yeAKYIDDSAQIVVPADLEEEqeeqiQELALKAYKALGCrGLARVDFfLTEDGEIVLNEVNTIPG 177
|
|
| ATPgrasp_ST |
pfam14397 |
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ... |
99-271 |
5.93e-07 |
|
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the biosynthesis of cell surface polysaccharides.
Pssm-ID: 405145 [Multi-domain] Cd Length: 278 Bit Score: 50.03 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 99 DKLRSLQLLARQGIDLPVT-GIAHSPDDTSDLIDMVGGAP--LVVKLVEGTQGIGVVLAETR-----QAAESVIDAFRGL 170
Cdd:pfam14397 21 DKLKFKQLALRAGLPVPKLyGVISIGHDISRLDAFVRSLPpgFVIKPAKGSGGKGILVITRRgdqdyFKSSGCRILLDEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 171 NAHI----------LVQEYIKEARG---------RDIRCLVV----GDEVVAAIERRAKEGDFRSNLHRGGMA------- 220
Cdd:pfam14397 101 KRHVsslggkpdvaLVEERIVQDPVfaklspesvNTIRVITFlldnGVPVMPAMLRLGTGASLVDNLHQGGVGvgidlat 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 221 ------SIASITPRER-----------------------EIAIKAAQTM-GLDVAGVDI-LRAERGPLVMEVNASPGLEG 269
Cdd:pfam14397 181 gvlfkpALQAVQYGEPiehhpdtgvkfrgfqipnwdqilELAAECAQTLpGLGYVGWDIvIDENGGPLLLELNARPGLGI 260
|
..
gi 581978245 270 VE 271
Cdd:pfam14397 261 FQ 262
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
93-292 |
1.82e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.08 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 93 AITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDmvGGA-PLVVKLVEGTQGIGVVLAETRQAA-ESVIDAFRGL 170
Cdd:PRK02186 101 AIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALD--GLTyPVVVKPRMGSGSVGVRLCASVAEAaAHCAALRRAG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 171 NAHILVQEYIkEARGRDIRCLVVGDEV-VAAIERRAKE---------GDFRSNLHRGGMASIASITPRereiaikAAQTM 240
Cdd:PRK02186 179 TRAALVQAYV-EGDEYSVETLTVARGHqVLGITRKHLGppphfveigHDFPAPLSAPQRERIVRTVLR-------ALDAV 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581978245 241 GLDV--AGVDILRAERGPLVMEVNasPGLEG------VEKTTGVDIAGRMIQ-WIERHATP 292
Cdd:PRK02186 251 GYAFgpAHTELRVRGDTVVIIEIN--PRLAGgmipvlLEEAFGVDLLDHVIDlHLGVAAFA 309
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
93-266 |
4.47e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 47.62 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 93 AITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVK--------LVEGTQGIGVVLAETRQAAESVI 164
Cdd:COG3919 111 LLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF-PVVVKpadsvgydELSFPGKKKVFYVDDREELLALL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 165 DAFRGLNAHILVQEYI--KEARGRDIRCLVVGD-EVVAAIERRAkegdFRSNLHRGGmASIASITPREREIaIKAAQTM- 240
Cdd:COG3919 190 RRIAAAGYELIVQEYIpgDDGEMRGLTAYVDRDgEVVATFTGRK----LRHYPPAGG-NSAARESVDDPEL-EEAARRLl 263
|
170 180 190
....*....|....*....|....*....|..
gi 581978245 241 -GLD---VAGVDILRAERG--PLVMEVNASPG 266
Cdd:COG3919 264 eALGyhgFANVEFKRDPRDgeYKLIEINPRFW 295
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1-263 |
1.49e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 45.65 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 1 MKIAILSRDGTLYSCKRLREAaMKRGHLVEI-LDPLS--CYMN----ISPAASSIHYKGRQLP-----HFDAVIPriGSA 68
Cdd:PRK12767 2 MNILVTSAGRRVQLVKALKKS-LLKGRVIGAdISELApaLYFAdkfyVVPKVTDPNYIDRLLDickkeKIDLLIP--LID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 69 ITFYGTAALRQ-FEMLGSYPLNESVA-ITRARDKLRSLQLLARQGIDLPVTGIAHSPDDTS-DLIDMVGGAPLVVKLVEG 145
Cdd:PRK12767 79 PELPLLAQNRDrFEEIGVKVLVSSKEvIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKaALAKGELQFPLFVKPRDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 146 TQGIGVVLAETRQAAESVIDafrgLNAHILVQEYIkeaRGRDIRCLVVGD---EVVAAIERRakegdfRSNLhRGGMASI 222
Cdd:PRK12767 159 SASIGVFKVNDKEELEFLLE----YVPNLIIQEFI---EGQEYTVDVLCDlngEVISIVPRK------RIEV-RAGETSK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 581978245 223 ASITPRER--EIAIKAAQTMG----LDvagVDILRAERGPLVMEVNA 263
Cdd:PRK12767 225 GVTVKDPElfKLAERLAEALGargpLN---IQCFVTDGEPYLFEINP 268
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
56-278 |
8.68e-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: 43.75 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 56 PHFDAVIPriGSAI-TFYGTAAL--RQFEMLGsyplNESVAITRARDKLRSLQLLARQGIDLPVTgIAHSPDDTSdlidm 132
Cdd:COG2232 72 DDPDGLVY--GSGFeNFPELLERlaRRLPLLG----NPPEVVRRVKDPLRFFALLDELGIPHPET-RFEPPPDPG----- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 133 vggaPLVVKLVEGTQGIGVVLAETRQAAEsvidafrglnAHILVQEYIKearGRDIRCLVVGD----EVVAAIE---RRA 205
Cdd:COG2232 140 ----PWLVKPIGGAGGWHIRPADSEAPPA----------PGRYFQRYVE---GTPASVLFLADgsdaRVLGFNRqliGPA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581978245 206 KEGDFRSnlhrGGMASIASITPREREIAIKAAQTM-------GLdvAGVDILRAERGPLVMEVNASPG--LEGVEKTTGV 276
Cdd:COG2232 203 GERPFRY----GGNIGPLALPPALAEEMRAIAEALvaalglvGL--NGVDFILDGDGPYVLEVNPRPQasLDLYEDATGG 276
|
..
gi 581978245 277 DI 278
Cdd:COG2232 277 NL 278
|
|
| |
