|
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: 601.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
4.80e-122 |
|
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: 350.49 E-value: 4.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 2 KIAILSRDGTLySCKRLREAAIQRGHLVEILDPLSCYMNINPaassihyKGRKLPHFDAVIPRIgtAITFYGTAALRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 82 MLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 162 SVIDAFRGLNA---HILVQEYIKEAQGCDIRCLVVGDEVVAAIERRaKEGDFRSNLHRGGAASVASITPQEREIAIKAAR 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 254797732 239 TMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-290 |
2.57e-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: 326.13 E-value: 2.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASsiHYKGRKLPHFDAVIPRIGTaiTFYGTAALRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 161 ESVIDAFRGL-NAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAART 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 254797732 240 MALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHA 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 |
8.04e-104 |
|
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: 300.96 E-value: 8.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 97 ARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 176 VQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 254797732 256 PLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
2.60e-49 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 165.49 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 2 KIAILSRDGTLYSCKRLREAAIQRGhlveiLDPLscYMNINPAASSIH------YKGRKLPHFDAVIPRIGTAITFYGTA 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 76 ----ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720 74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQ 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 254797732 229 EREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIE 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: 601.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
4.80e-122 |
|
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: 350.49 E-value: 4.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 2 KIAILSRDGTLySCKRLREAAIQRGHLVEILDPLSCYMNINPaassihyKGRKLPHFDAVIPRIgtAITFYGTAALRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 82 MLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 162 SVIDAFRGLNA---HILVQEYIKEAQGCDIRCLVVGDEVVAAIERRaKEGDFRSNLHRGGAASVASITPQEREIAIKAAR 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 254797732 239 TMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-290 |
2.57e-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: 326.13 E-value: 2.57e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASsiHYKGRKLPHFDAVIPRIGTaiTFYGTAALRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 161 ESVIDAFRGL-NAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAART 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 254797732 240 MALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHA 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 |
8.04e-104 |
|
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: 300.96 E-value: 8.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 97 ARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 176 VQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 254797732 256 PLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 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 |
4.29e-57 |
|
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: 178.82 E-value: 4.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
Cdd:pfam18030 1 MKIAILSRNPNLYSTRRLVEAAEARGHEVEVIDPLRCYMNIESGKPEIHYKGEPLPDFDAVIPRIGASITFYGTAVLRQF 80
|
90
....*....|....
gi 254797732 81 EMLGSYPLNESVAI 94
Cdd:pfam18030 81 EMMGVFSLNSSQAI 94
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
2.60e-49 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 165.49 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 2 KIAILSRDGTLYSCKRLREAAIQRGhlveiLDPLscYMNINPAASSIH------YKGRKLPHFDAVIPRIGTAITFYGTA 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 76 ----ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720 74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQ 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 254797732 229 EREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIE 287
Cdd:NF040720 232 QEELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 290
|
|
| PRK12458 |
PRK12458 |
glutathione synthetase; Provisional |
88-288 |
3.07e-21 |
|
glutathione synthetase; Provisional
Pssm-ID: 183536 [Multi-domain] Cd Length: 338 Bit Score: 92.01 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 88 LNESVAIARARDKLRSMQLlarQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAET--RQAAESVID 165
Cdd:PRK12458 118 VNDPDGLRIANNKLYFQSF---PEEVRPTTHISRNKEYIREFLEESPGDKMILKPLQGSGGQGVFLIEKsaQSNLNQILE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 166 AFRGLNaHILVQEYIKEAQGCDIRCLVV------GDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAART 239
Cdd:PRK12458 195 FYSGDG-YVIAQEYLPGAEEGDVRILLLngepleRDGHYAAMRRVPAGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPK 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 254797732 240 MALD---VAGVDILranrGPLVMEVNA-SP-GLEGIEKTTGIDIAGKMIRWIER 288
Cdd:PRK12458 274 LVRDglfFVGLDIV----GDKLVEVNVfSPgGLTRINKLNKIDFVEDIIEALER 323
|
|
| PRK05246 |
PRK05246 |
glutathione synthetase; Provisional |
174-288 |
1.27e-17 |
|
glutathione synthetase; Provisional
Pssm-ID: 235371 [Multi-domain] Cd Length: 316 Bit Score: 81.30 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 174 ILVQEYIKEAQGCDIRCLVVGDEVV-AAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMA---LDVAGVDI 249
Cdd:PRK05246 195 VMAQRYLPEIKEGDKRILLVDGEPVgYALARIPAGGETRGNLAAGGRGEATPLTERDREICAAIGPELKergLIFVGIDV 274
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254797732 250 LranrGPLVMEVN-ASP-GLEGIEKTTGIDIAGKMIRWIER 288
Cdd:PRK05246 275 I----GDYLTEINvTSPtGIREIERLTGVDIAGMLWDAIEA 311
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
91-267 |
4.26e-17 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 81.36 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 91 SVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVL-AETRQAAESVIDAFRG 169
Cdd:PRK14016 206 AIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGY-PVVVKPLDGNHGRGVTVnITTREEIEAAYAVASK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 170 LNAHILVQEYIKeaqGCDIRCLVVGDEVVAAIERRAKE--GDFRS----------------------------------- 212
Cdd:PRK14016 285 ESSDVIVERYIP---GKDHRLLVVGGKLVAAARREPPHviGDGKHtirelieivnqdprrgeghekpltkiklddialle 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 213 ------------------------NLHRGGAAS--VASITPQEREIAIKAARTMALDVAGVDI--------LRANRGpLV 258
Cdd:PRK14016 362 lakqgytldsvppkgekvylrrnaNLSTGGTAIdvTDEVHPENAAIAERAAKIIGLDIAGVDVvcediskpLEEQGG-AI 440
|
....*....
gi 254797732 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 |
6.12e-14 |
|
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: 70.29 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 58 FDAVIPriGTAITFYGTAALRqfEMLGsYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaP 137
Cdd:COG0439 18 IDAVLS--ESEFAVETAAELA--EELG-LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGY-P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 138 LVVKLVEGTQGIGVVLAETRQAAESVIDAFRG------LNAHILVQEYIkEAQGCDIRCLVVGDEVV-AAIERRAKEGDF 210
Cdd:COG0439 92 VVVKPADGAGSRGVRVVRDEEELEAALAEARAeakagsPNGEVLVEEFL-EGREYSVEGLVRDGEVVvCSITRKHQKPPY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 211 RsnLHRGGAASvASITPQEREIAIKAARTmALDVAGVD--------ILRANRGPLVMEVNASPGLEGI----EKTTGIDI 278
Cdd:COG0439 171 F--VELGHEAP-SPLPEELRAEIGELVAR-ALRALGYRrgafhtefLLTPDGEPYLIEINARLGGEHIppltELATGVDL 246
|
....*.
gi 254797732 279 AGKMIR 284
Cdd:COG0439 247 VREQIR 252
|
|
| GSH-S_ATP |
pfam02955 |
Prokaryotic glutathione synthetase, ATP-grasp domain; |
139-275 |
1.74e-12 |
|
Prokaryotic glutathione synthetase, ATP-grasp domain;
Pssm-ID: 427078 [Multi-domain] Cd Length: 175 Bit Score: 64.50 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 139 VVKLVEGTQGIGVV-LAETRQAAESVIDAFRGL-NAHILVQEYIKEAQGCDIRCLVVGDEVV-AAIERRAKEGDFRSNLH 215
Cdd:pfam02955 35 ILKPLDGMGGAGIFrVKKGDPNLNVILETLTQYgTRPVMAQRYLPEIKEGDKRILLINGEPIgYALARIPAAGEFRGNLA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254797732 216 RGGAASVASITPQEREIAIKAARTMA---LDVAGVDILranrGPLVMEVN-ASP-GLEGIEKTTG 275
Cdd:pfam02955 115 AGGRGEATPLTERDREICETIGPKLKergLFFVGLDVI----GDYLTEINvTSPtGIREIERLTG 175
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
80-267 |
5.62e-12 |
|
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: 65.13 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 80 FEML-----GSYPLnesvAIARARDKLRSMQLLARQGIDLPvTGIAHSPDDTSDLIDMVG--GAPLVVKLV-EGTqGIGV 151
Cdd:COG1181 75 LELLgipytGSGVL----ASALAMDKALTKRVLAAAGLPTP-PYVVLRRGELADLEAIEEelGLPLFVKPArEGS-SVGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 152 VLAETRQAAESVIDAFRGLNAHILVQEYIKeaqGCDIRCLVVGDEVVAA---IERRAKEG--DFRSNLHRGGAASV--AS 224
Cdd:COG1181 149 SKVKNAEELAAALEEAFKYDDKVLVEEFID---GREVTVGVLGNGGPRAlppIEIVPENGfyDYEAKYTDGGTEYIcpAR 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254797732 225 ITPQE----REIAIKAARtmALDVAG---VD-ILRANRGPLVMEVNASPGL 267
Cdd:COG1181 226 LPEELeeriQELALKAFR--ALGCRGyarVDfRLDEDGEPYLLEVNTLPGM 274
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
99-267 |
2.37e-09 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 57.04 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 99 DKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQA-AESVIDAFRgLNAHILVQ 177
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLG-LPLVVKPAREGSSVGVSKVKEEDElQAALELAFK-YDDEVLVE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 178 EYIKeaqGCDIRCLVVGDEVVAAIERRAKEG--DFRSNLHRGGAASV------ASITPQEREIAIKAARtmALDVAG--- 246
Cdd:PRK01372 176 KYIK---GRELTVAVLGGKALPVIEIVPAGEfyDYEAKYLAGGTQYIcpaglpAEIEAELQELALKAYR--ALGCRGwgr 250
|
170 180
....*....|....*....|..
gi 254797732 247 VD-ILRANRGPLVMEVNASPGL 267
Cdd:PRK01372 251 VDfMLDEDGKPYLLEVNTQPGM 272
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
93-284 |
6.19e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 56.78 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 93 AIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDmvGGA-PLVVKLVEGTQGIGVVLAETRQAA-ESVIDAFRGL 170
Cdd:PRK02186 101 AIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALD--GLTyPVVVKPRMGSGSVGVRLCASVAEAaAHCAALRRAG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 171 NAHILVQEYIKEAQ-GCDIRCLVVGDEVVAAIERR-AKEGDFRSNLHRGGAASVAsitPQEREIAIKAARtmALDVAG-- 246
Cdd:PRK02186 179 TRAALVQAYVEGDEySVETLTVARGHQVLGITRKHlGPPPHFVEIGHDFPAPLSA---PQRERIVRTVLR--ALDAVGya 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254797732 247 -----VDILRANRGPLVMEVNasPGLEG------IEKTTGIDIAGKMIR 284
Cdd:PRK02186 254 fgpahTELRVRGDTVVIIEIN--PRLAGgmipvlLEEAFGVDLLDHVID 300
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-263 |
5.77e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 53.35 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 57 HFDAVIPRIGTAITFYgtAALRQ-FEMLGSYPLNESVA-IARARDKLRSMQLLARQGIDLPVTGIAHSPDDTS-DLIDMV 133
Cdd:PRK12767 69 KIDLLIPLIDPELPLL--AQNRDrFEEIGVKVLVSSKEvIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKaALAKGE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 134 GGAPLVVKLVEGTQGIGVVLAETRQAAESVIDafrgLNAHILVQEYIKEAQ-GCDIRCLVVGdEVVAAIERRakegdfRS 212
Cdd:PRK12767 147 LQFPLFVKPRDGSASIGVFKVNDKEELEFLLE----YVPNLIIQEFIEGQEyTVDVLCDLNG-EVISIVPRK------RI 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254797732 213 NLhRGGAASVASITPQER--EIAIKAARtmALDVAG---VDILRANRGPLVMEVNA 263
Cdd:PRK12767 216 EV-RAGETSKGVTVKDPElfKLAERLAE--ALGARGplnIQCFVTDGEPYLFEINP 268
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
97-266 |
9.95e-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: 50.46 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 97 ARDKLRSMQLLARQGIDLPVTGIAHSPDdtsdlidmVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDafrglnaHILV 176
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQAEELL--------REEKKYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 177 QEYIKE--------AQGCDIRCLVVGDEVvaaIERRAKEGDFRSNLhrggaasVASITPqEREIAIKAARTMALDV---- 244
Cdd:pfam02655 66 QEFIEGeplsvsllSDGEKALPLSVNRQY---IDNGGSGFVYAGNV-------TPSRTE-LKEEIIELAEEVVECLpglr 134
|
170 180
....*....|....*....|....
gi 254797732 245 --AGVDILRANRGPLVMEVNASPG 266
Cdd:pfam02655 135 gyVGVDLVLKDNEPYVIEVNPRIT 158
|
|
| ATPgrasp_YheCD |
pfam14398 |
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ... |
124-266 |
7.18e-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: 49.48 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 124 DDTSDLIDMVGGAPLV-VKLVEGTQGIGVVLAE------------TRQAAESVIDAFRGLNAHI---------LVQEYIK 181
Cdd:pfam14398 36 QSPEDLERMLEKYGSVyLKPVNGSLGKGILRIEkdgggyylygryGKNSKTNRFLDFSELESFLrrllgkkryIIQQGID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 182 --EAQGC--DIRCLVVGDE-----VVAAIERRAKEGDFRSNLHRGGAASVAS-----ITPQEREIAIKA-ARTMALDVA- 245
Cdd:pfam14398 116 laTIDGRpfDFRVLVQKNGkgkwvVTGIAARIAGPGSITTNLSGGGTAIPLEealrrAFGEERAEKILEkLEELALELAr 195
|
170 180 190
....*....|....*....|....*....|....
gi 254797732 246 ------------GVDILRANRGPLVM-EVNASPG 266
Cdd:pfam14398 196 aleesfgglgelGLDLGIDKNGRVWLlEVNSKPG 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 |
7.76e-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: 48.85 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 135 GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIKeaqGCDIRCLVVGDE---VVAAIERRAKEG--D 209
Cdd:pfam07478 36 GYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIE---GREIECAVLGNEdpeVSPVGEIVPSGGfyD 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254797732 210 FRSNLHRGGAASV--ASITPQE----REIAIKAARtmALDVAG---VDI-LRANRGPLVMEVNASPG 266
Cdd:pfam07478 113 YEAKYIDDSAQIVvpADLEEEQeeqiQELALKAYK--ALGCRGlarVDFfLTEDGEIVLNEVNTIPG 177
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
93-266 |
1.24e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 49.16 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 93 AIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVK--------LVEGTQGIGVVLAETRQAAESVI 164
Cdd:COG3919 111 LLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF-PVVVKpadsvgydELSFPGKKKVFYVDDREELLALL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 165 DAFRGLNAHILVQEYIKEAQGcDIRCLVV-----GDEVVAAIERRAKEgdfrsnLHRGGAASVASITPQEREIaIKAART 239
Cdd:COG3919 190 RRIAAAGYELIVQEYIPGDDG-EMRGLTAyvdrdGEVVATFTGRKLRH------YPPAGGNSAARESVDDPEL-EEAARR 261
|
170 180 190
....*....|....*....|....*....|....
gi 254797732 240 M--ALD---VAGVDILRANRG--PLVMEVNASPG 266
Cdd:COG3919 262 LleALGyhgFANVEFKRDPRDgeYKLIEINPRFW 295
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
78-278 |
6.23e-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: 44.14 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 78 RQFEMLGsyplNESVAIARARDKLRSMQLLARQGIDLPVTgIAHSPDDTSdlidmvggaPLVVKLVEGTQGIGVVLAETR 157
Cdd:COG2232 95 RRLPLLG----NPPEVVRRVKDPLRFFALLDELGIPHPET-RFEPPPDPG---------PWLVKPIGGAGGWHIRPADSE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 158 QAAEsvidafrglnAHILVQEYIkeaQGCDIRCLVVGD----EVVAAIE---RRAKEGDFRSnlhrGGAASVASITPQER 230
Cdd:COG2232 161 APPA----------PGRYFQRYV---EGTPASVLFLADgsdaRVLGFNRqliGPAGERPFRY----GGNIGPLALPPALA 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254797732 231 EIAIKAARTMALD-----VAGVDILRANRGPLVMEVNASPG--LEGIEKTTGIDI 278
Cdd:COG2232 224 EEMRAIAEALVAAlglvgLNGVDFILDGDGPYVLEVNPRPQasLDLYEDATGGNL 278
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
93-284 |
4.66e-04 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 41.91 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 93 AIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVgGAPLVVK--LVEGTQGIGVVLAEtRQAAESVIDAFRGL 170
Cdd:TIGR01369 663 SIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEI-GYPVLVRpsYVLGGRAMEIVYNE-EELRRYLEEAVAVS 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 171 NAH-ILVQEYIKEAQGCDIRCLVVGDEVVAA-----IErrakegdfRSNLHRGGAASV--ASITPQEREIAIKA-ARTMA 241
Cdd:TIGR01369 741 PEHpVLIDKYLEDAVEVDVDAVSDGEEVLIPgimehIE--------EAGVHSGDSTCVlpPQTLSAEIVDRIKDiVRKIA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 254797732 242 --LDVAG---VDILRANRGPLVMEVN--ASPGLEGIEKTTGIDIAGKMIR 284
Cdd:TIGR01369 813 keLNVKGlmnIQFAVKDGEVYVIEVNprASRTVPFVSKATGVPLAKLAVR 862
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
92-269 |
1.01e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 40.27 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 92 VAIARARDKLRSMQLLARQGI------DLPVTGIAHSPDDTsdLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVI 164
Cdd:PRK14572 123 LASALAMDKTRANQIFLQSGQkvapffELEKLKYLNSPRKT--LLKLESlGFPQFLKPVEGGSSVSTYKITNAEQLMTLL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 165 DAFRGLNAHILVQEyikeaqgcdircLVVGDEVVAAIERRAKEG-------------------DFRSNLHRGGAASV--A 223
Cdd:PRK14572 201 ALIFESDSKVMSQS------------FLSGTEVSCGVLERYRGGkrnpialpateivpggeffDFESKYKQGGSEEItpA 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254797732 224 SITPQE----REIAIKAARTMALD-VAGVDILRANRGPLVMEVNASPGLEG 269
Cdd:PRK14572 269 RISDQEmkrvQELAIRAHESLGCKgYSRTDFIIVDGEPHILETNTLPGMTE 319
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
93-247 |
7.15e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 37.44 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 93 AIARARDKLRSMQLLARQGIdlPVTG--IAHSPDDTSDLIDMVGGaPLVVKLV-EGTQGIGVVLAETRQAAESVIDAFRG 169
Cdd:PRK06019 94 ALAIAQDRLTEKQFLDKLGI--PVAPfaVVDSAEDLEAALADLGL-PAVLKTRrGGYDGKGQWVIRSAEDLEAAWALLGS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254797732 170 LNAhiLVQEYI---KEAQgcdirclvvgdeVVAAierRAKEGDFRS-----NLHRGG--AASV--ASITPQEREIAIKAA 237
Cdd:PRK06019 171 VPC--ILEEFVpfeREVS------------VIVA---RGRDGEVVFyplveNVHRNGilRTSIapARISAELQAQAEEIA 233
|
170
....*....|..
gi 254797732 238 RTMA--LDVAGV 247
Cdd:PRK06019 234 SRIAeeLDYVGV 245
|
|
| |
