|
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: 604.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 1 MKIAILSRDGTLYSCKRLREAAMRRGHLVEILDPLSCYMNINPAASSIHYKGRRLPHYDAVIPRIGSAITFYGTAALRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 161 ESVIDAFRGLNAHILVQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQTL 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 241 GLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWIERHATPEFCLKIGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
5.16e-114 |
|
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: 330.08 E-value: 5.16e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 2 KIAILSRDGTLySCKRLREAAMRRGHLVEILDPLSCYMNINPaassihyKGRRLPHYDAVIPRIgsAITFYGTAALRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 82 LLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 162 SVIDAFRGLNA---HILVQEYIAEAKGCDIRCLVVGNEVVAAIERCaKAGDFRSNLHRGGVASIATITPRERDIAIKAAQ 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446607020 239 TLGLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-290 |
2.63e-111 |
|
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: 323.82 E-value: 2.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 1 MKIAILSRDGTLYSCKRLREAAMRRGHLVEILDPLSCYMNINPAASsiHYKGRRLPHYDAVIPRIGSaiTFYGTAALRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 161 ESVIDAFRGL-NAHILVQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQT 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446607020 240 LGLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWIERHA 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 |
1.68e-95 |
|
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: 279.77 E-value: 1.68e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 97 ARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 176 VQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQTLGLDVAGVDILRAARG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 446607020 256 PLVMEVNASPGLEGIEKTTGVDIAGRMIQWI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
6.03e-46 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 156.63 E-value: 6.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 2 KIAILSRDGTLYSCKRLREAAMRRGhlveiLDPLscYMNINPAASSIH------YKGRRLPHYDAVIPRIGSAITFYGTA 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 76 ----ALRQFELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720 74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPR 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446607020 229 ERDIAIKAAQTLGLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWIE 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: 604.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 1 MKIAILSRDGTLYSCKRLREAAMRRGHLVEILDPLSCYMNINPAASSIHYKGRRLPHYDAVIPRIGSAITFYGTAALRQF 80
Cdd:PRK10446 1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446 81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 161 ESVIDAFRGLNAHILVQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQTL 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 241 GLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWIERHATPEFCLKIGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
2-286 |
5.16e-114 |
|
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: 330.08 E-value: 5.16e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 2 KIAILSRDGTLySCKRLREAAMRRGHLVEILDPLSCYMNINPaassihyKGRRLPHYDAVIPRIgsAITFYGTAALRQFE 81
Cdd:TIGR00768 1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 82 LLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768 71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 162 SVIDAFRGLNA---HILVQEYIAEAKGCDIRCLVVGNEVVAAIERCaKAGDFRSNLHRGGVASIATITPRERDIAIKAAQ 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446607020 239 TLGLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-290 |
2.63e-111 |
|
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: 323.82 E-value: 2.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 1 MKIAILSRDGTLYSCKRLREAAMRRGHLVEILDPLSCYMNINPAASsiHYKGRRLPHYDAVIPRIGSaiTFYGTAALRQF 80
Cdd:COG0189 2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 81 ELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189 78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 161 ESVIDAFRGL-NAHILVQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQT 239
Cdd:COG0189 157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446607020 240 LGLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWIERHA 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 |
1.68e-95 |
|
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: 279.77 E-value: 1.68e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 97 ARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443 1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 176 VQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQTLGLDVAGVDILRAARG 255
Cdd:pfam08443 78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157
|
170 180 190
....*....|....*....|....*....|.
gi 446607020 256 PLVMEVNASPGLEGIEKTTGVDIAGRMIQWI 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 |
4.72e-55 |
|
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: 173.43 E-value: 4.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 1 MKIAILSRDGTLYSCKRLREAAMRRGHLVEILDPLSCYMNINPAASSIHYKGRRLPHYDAVIPRIGSAITFYGTAALRQF 80
Cdd:pfam18030 1 MKIAILSRNPNLYSTRRLVEAAEARGHEVEVIDPLRCYMNIESGKPEIHYKGEPLPDFDAVIPRIGASITFYGTAVLRQF 80
|
90
....*....|....
gi 446607020 81 ELLGSYPLNESVAI 94
Cdd:pfam18030 81 EMMGVFSLNSSQAI 94
|
|
| MptN_Meth |
NF040720 |
tetrahydromethanopterin:alpha-L-glutamate ligase; |
2-287 |
6.03e-46 |
|
tetrahydromethanopterin:alpha-L-glutamate ligase;
Pssm-ID: 468684 [Multi-domain] Cd Length: 290 Bit Score: 156.63 E-value: 6.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 2 KIAILSRDGTLYSCKRLREAAMRRGhlveiLDPLscYMNINPAASSIH------YKGRRLPHYDAVIPRIGSAITFYGTA 75
Cdd:NF040720 1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 76 ----ALRQFELLGSYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720 74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIAEAKGCDIRCLVVGNEVVAAIERCAKAGDFRSNLHRGGVASIATITPR 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446607020 229 ERDIAIKAAQTLGLDVAGVDILRAARGPLVMEVNASPGLEGIEKTTGVDIAGRMIQWIE 287
Cdd:NF040720 232 QEELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 290
|
|
| PRK12458 |
PRK12458 |
glutathione synthetase; Provisional |
115-288 |
4.68e-20 |
|
glutathione synthetase; Provisional
Pssm-ID: 183536 [Multi-domain] Cd Length: 338 Bit Score: 88.54 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 115 PITGIAHSPDDTSDLIKMVGGAPLVVKLVEGTQGIGVVLAET--RQAAESVIDAFRGLNaHILVQEYIAEAKGCDIRCLV 192
Cdd:PRK12458 142 PTTHISRNKEYIREFLEESPGDKMILKPLQGSGGQGVFLIEKsaQSNLNQILEFYSGDG-YVIAQEYLPGAEEGDVRILL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 193 VGNE------VVAAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQTL---GLDVAGVDILraarGPLVMEVNA 263
Cdd:PRK12458 221 LNGEplerdgHYAAMRRVPAGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPKLvrdGLFFVGLDIV----GDKLVEVNV 296
|
170 180
....*....|....*....|....*..
gi 446607020 264 -SP-GLEGIEKTTGVDIAGRMIQWIER 288
Cdd:PRK12458 297 fSPgGLTRINKLNKIDFVEDIIEALER 323
|
|
| PRK05246 |
PRK05246 |
glutathione synthetase; Provisional |
174-288 |
1.29e-19 |
|
glutathione synthetase; Provisional
Pssm-ID: 235371 [Multi-domain] Cd Length: 316 Bit Score: 87.07 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 174 ILVQEYIAEAKGCDIRCLVVGNEVV-AAIERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQTL---GLDVAGVDI 249
Cdd:PRK05246 195 VMAQRYLPEIKEGDKRILLVDGEPVgYALARIPAGGETRGNLAAGGRGEATPLTERDREICAAIGPELkerGLIFVGIDV 274
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446607020 250 LraarGPLVMEVN-ASP-GLEGIEKTTGVDIAGRMIQWIER 288
Cdd:PRK05246 275 I----GDYLTEINvTSPtGIREIERLTGVDIAGMLWDAIEA 311
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
91-267 |
1.34e-17 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 82.90 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 91 SVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGaPLVVKLVEGTQGIGVVL-AETRQAAESVIDAFRG 169
Cdd:PRK14016 206 AIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGY-PVVVKPLDGNHGRGVTVnITTREEIEAAYAVASK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 170 LNAHILVQEYIaeaKGCDIRCLVVGNEVVAAIERCAK--AGDFRS----------------------------------- 212
Cdd:PRK14016 285 ESSDVIVERYI---PGKDHRLLVVGGKLVAAARREPPhvIGDGKHtirelieivnqdprrgeghekpltkiklddialle 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 213 ------------------------NLHRGGVASIAT--ITPRERDIAIKAAQTLGLDVAGVDI--------LRAARGpLV 258
Cdd:PRK14016 362 lakqgytldsvppkgekvylrrnaNLSTGGTAIDVTdeVHPENAAIAERAAKIIGLDIAGVDVvcediskpLEEQGG-AI 440
|
....*....
gi 446607020 259 MEVNASPGL 267
Cdd:PRK14016 441 VEVNAAPGL 449
|
|
| GSH-S_ATP |
pfam02955 |
Prokaryotic glutathione synthetase, ATP-grasp domain; |
139-275 |
1.94e-14 |
|
Prokaryotic glutathione synthetase, ATP-grasp domain;
Pssm-ID: 427078 [Multi-domain] Cd Length: 175 Bit Score: 69.90 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 139 VVKLVEGTQGIGVV-LAETRQAAESVIDAFRGL-NAHILVQEYIAEAKGCDIRCLVVGNEVV-AAIERCAKAGDFRSNLH 215
Cdd:pfam02955 35 ILKPLDGMGGAGIFrVKKGDPNLNVILETLTQYgTRPVMAQRYLPEIKEGDKRILLINGEPIgYALARIPAAGEFRGNLA 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446607020 216 RGGVASIATITPRERDIAIKAAQTL---GLDVAGVDILraarGPLVMEVN-ASP-GLEGIEKTTG 275
Cdd:pfam02955 115 AGGRGEATPLTERDREICETIGPKLkerGLFFVGLDVI----GDYLTEINvTSPtGIREIERLTG 175
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
59-284 |
1.81e-13 |
|
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: 68.75 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 59 DAVIPriGSAITFYGTAALRqfELLGsYPLNESVAITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGaPL 138
Cdd:COG0439 19 DAVLS--ESEFAVETAAELA--EELG-LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGY-PV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 139 VVKLVEGTQGIGVVLAETRQAAESVIDAFRG------LNAHILVQEYIaEAKGCDIRCLVVGNEVV-AAIERCAKAGDFR 211
Cdd:COG0439 93 VVKPADGAGSRGVRVVRDEEELEAALAEARAeakagsPNGEVLVEEFL-EGREYSVEGLVRDGEVVvCSITRKHQKPPYF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 212 snLHRGGVASiATITPRER----DIAIKAAQTLGLD--VAGVDILRAARG-PLVMEVNASPGLEGI----EKTTGVDIAG 280
Cdd:COG0439 172 --VELGHEAP-SPLPEELRaeigELVARALRALGYRrgAFHTEFLLTPDGePYLIEINARLGGEHIppltELATGVDLVR 248
|
....
gi 446607020 281 RMIQ 284
Cdd:COG0439 249 EQIR 252
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
97-267 |
3.47e-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: 65.51 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 97 ARDKLRSLQLLARQGIDLPiTGIAHSPDDTSDLIKMVG--GAPLVVKLV-EGTqGIGVVLAETRQAAESVIDAFRGLNAH 173
Cdd:COG1181 93 AMDKALTKRVLAAAGLPTP-PYVVLRRGELADLEAIEEelGLPLFVKPArEGS-SVGVSKVKNAEELAAALEEAFKYDDK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 174 ILVQEYIaeaKGCDIRCLVVGNEVVAA---IERCAKAG--DFRSNLHRGGVASI--ATITPRE----RDIAIKAAQTLGL 242
Cdd:COG1181 171 VLVEEFI---DGREVTVGVLGNGGPRAlppIEIVPENGfyDYEAKYTDGGTEYIcpARLPEELeeriQELALKAFRALGC 247
|
170 180
....*....|....*....|....*..
gi 446607020 243 -DVAGVD-ILRAARGPLVMEVNASPGL 267
Cdd:COG1181 248 rGYARVDfRLDEDGEPYLLEVNTLPGM 274
|
|
| MfnD |
COG1821 |
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme ... |
82-284 |
1.07e-08 |
|
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme transport and metabolism];
Pssm-ID: 441426 [Multi-domain] Cd Length: 323 Bit Score: 55.32 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 82 LLGSYPlnESVAItrARDKLRSLQLLARQGID-LPITGIAHSPDDTSDlikmvggaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG1821 111 NLGSSP--EAIAL--AADKLLTAELLAAAGIPtPPTFPADDAPPLLAG--------PWVVKPDDGAGSEGTRLFDDPAAL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 161 ESVIDAFRGLnahiLVQEYIA-EAkgCDIRCLVVGNEVV---AAIERCAKAGDfRSNLHRGGVASIATITPRERDIAIKA 236
Cdd:COG1821 179 RAREARGAGL----IVQPYIEgEA--ASLSLLCGRGGALllsINRQRIEVDGG-RFSYLGGTVPAEHPRKEELQALAQKV 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446607020 237 AQTL----GLdvAGVDILRAARGPLVMEVNASP--GLEGIEKTTGVDIAGRMIQ 284
Cdd:COG1821 252 AEALpglrGY--VGVDLILTADGPVVVEVNPRLttSYVGLRAALGENLAALLLD 303
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
99-267 |
1.30e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 55.12 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 99 DKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGgAPLVVKLVEGTQGIGVVLAETRQA-AESVIDAFRgLNAHILVQ 177
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLG-LPLVVKPAREGSSVGVSKVKEEDElQAALELAFK-YDDEVLVE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 178 EYIaeaKGCDIRCLVVGNEVVAAIERCAKAG--DFRSNLHRGGVASI------ATITPRERDIAIKAAQTLGLDVAG-VD 248
Cdd:PRK01372 176 KYI---KGRELTVAVLGGKALPVIEIVPAGEfyDYEAKYLAGGTQYIcpaglpAEIEAELQELALKAYRALGCRGWGrVD 252
|
170 180
....*....|....*....|
gi 446607020 249 -ILRAARGPLVMEVNASPGL 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 |
2.00e-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: 52.77 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 97 ARDKLRSLQLLARQGIDLPITgiahspddTSDLIKMVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDafrglnaHILV 176
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPET--------LQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 177 QEYIaEAKGCDIRCLVVGNEVV------AAIERCAkagdfRSNLHRGGVASIATITPRE-RDIAIKAAQTL-GL-DVAGV 247
Cdd:pfam02655 66 QEFI-EGEPLSVSLLSDGEKALplsvnrQYIDNGG-----SGFVYAGNVTPSRTELKEEiIELAEEVVECLpGLrGYVGV 139
|
170
....*....|....*....
gi 446607020 248 DILRAARGPLVMEVNASPG 266
Cdd:pfam02655 140 DLVLKDNEPYVIEVNPRIT 158
|
|
| ATPgrasp_ST |
pfam14397 |
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ... |
99-267 |
3.32e-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: 50.42 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 99 DKLRSLQLLARQGIDLPIT-GIAHSPDDTSDLIKMVGGAP--LVVKLVEGTQGIGVVLAETR-----QAAESVIDAFRGL 170
Cdd:pfam14397 21 DKLKFKQLALRAGLPVPKLyGVISIGHDISRLDAFVRSLPpgFVIKPAKGSGGKGILVITRRgdqdyFKSSGCRILLDEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 171 NAHI----------LVQEYIAEAKGC---------DIRCLVV----GNEVVAAIERCAKAGDFRSNLHRGGVA---SIAT 224
Cdd:pfam14397 101 KRHVsslggkpdvaLVEERIVQDPVFaklspesvnTIRVITFlldnGVPVMPAMLRLGTGASLVDNLHQGGVGvgiDLAT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446607020 225 IT---------------------------------PRERDIAIKAAQTL-GLDVAGVDI-LRAARGPLVMEVNASPGL 267
Cdd:pfam14397 181 GVlfkpalqavqygepiehhpdtgvkfrgfqipnwDQILELAAECAQTLpGLGYVGWDIvIDENGGPLLLELNARPGL 258
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
94-263 |
4.25e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 50.65 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 94 ITRARDKLRSLQLLARQGIDLPITGIAHSPDDTS-DLIKMVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDafrgLNA 172
Cdd:PRK12767 106 IEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKaALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLE----YVP 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 173 HILVQEYIAEAK-GCDIRCLVVGNeVVAAIERcaKAGDFRSnlhrGGVA-SIATITPRERDIAIKAAQTLG----LDvag 246
Cdd:PRK12767 182 NLIIQEFIEGQEyTVDVLCDLNGE-VISIVPR--KRIEVRA----GETSkGVTVKDPELFKLAERLAEALGargpLN--- 251
|
170
....*....|....*..
gi 446607020 247 VDILRAARGPLVMEVNA 263
Cdd:PRK12767 252 IQCFVTDGEPYLFEINP 268
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
93-292 |
4.03e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 48.30 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 93 AITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKmvGGA-PLVVKLVEGTQGIGVVLAETRQAA-ESVIDAFRGL 170
Cdd:PRK02186 101 AIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALD--GLTyPVVVKPRMGSGSVGVRLCASVAEAaAHCAALRRAG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 171 NAHILVQEYIAEAK-GCDIRCLVVGNEVVAAI-ERCAKAGDFRSNLHRGGVASIATITPRERDIAIKAAQTLGLDV--AG 246
Cdd:PRK02186 179 TRAALVQAYVEGDEySVETLTVARGHQVLGITrKHLGPPPHFVEIGHDFPAPLSAPQRERIVRTVLRALDAVGYAFgpAH 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446607020 247 VDILRAARGPLVMEVNasPGLEG------IEKTTGVDIAGRMIQ-WIERHATP 292
Cdd:PRK02186 259 TELRVRGDTVVIIEIN--PRLAGgmipvlLEEAFGVDLLDHVIDlHLGVAAFA 309
|
|
| ATPgrasp_YheCD |
pfam14398 |
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ... |
124-266 |
6.54e-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: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 124 DDTSDLIKMVGGAPLV-VKLVEGTQGIGVVLAE------------TRQAAESVIDAFRGLNAHI---------LVQEYI- 180
Cdd:pfam14398 36 QSPEDLERMLEKYGSVyLKPVNGSLGKGILRIEkdgggyylygryGKNSKTNRFLDFSELESFLrrllgkkryIIQQGId 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 181 -AEAKGC--DIRCLVVGNE-----VVAAIERCAKAGDFRSNLHRGGVAS--------------IATITPRERDIAIKAAQ 238
Cdd:pfam14398 116 lATIDGRpfDFRVLVQKNGkgkwvVTGIAARIAGPGSITTNLSGGGTAIpleealrrafgeerAEKILEKLEELALELAR 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 446607020 239 T----------LGLDVaGVDIlraaRGPLVM-EVNASPG 266
Cdd:pfam14398 196 AleesfgglgeLGLDL-GIDK----NGRVWLlEVNSKPG 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 |
1.12e-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: 45.39 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 135 GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIaeaKGCDIRCLVVGNE--VVAAIERCAKAGDF-- 210
Cdd:pfam07478 36 GYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGI---EGREIECAVLGNEdpEVSPVGEIVPSGGFyd 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446607020 211 --RSNLHRGGVASIATITPRE-----RDIAIKAAQTLGL-DVAGVDI-LRAARGPLVMEVNASPG 266
Cdd:pfam07478 113 yeAKYIDDSAQIVVPADLEEEqeeqiQELALKAYKALGCrGLARVDFfLTEDGEIVLNEVNTIPG 177
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
93-266 |
3.86e-05 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 44.53 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 93 AITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVGGaPLVVK--------LVEGTQGIGVVLAETRQAAESVI 164
Cdd:COG3919 111 LLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF-PVVVKpadsvgydELSFPGKKKVFYVDDREELLALL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 165 DAFRGLNAHILVQEYIAEAKGcDIRCLVV-----GNEVVAAIERCakagdFRSNLHRGGVASIATITPRE--RDIAIKAA 237
Cdd:COG3919 190 RRIAAAGYELIVQEYIPGDDG-EMRGLTAyvdrdGEVVATFTGRK-----LRHYPPAGGNSAARESVDDPelEEAARRLL 263
|
170 180 190
....*....|....*....|....*....|..
gi 446607020 238 QTLGLD-VAGVDILRAARG--PLVMEVNASPG 266
Cdd:COG3919 264 EALGYHgFANVEFKRDPRDgeYKLIEINPRFW 295
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
93-283 |
1.19e-03 |
|
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: 40.37 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 93 AITRARDKLRSLQLLARQGIDLPITGIAHSPDDTSDLIKMVgGAPLVVK--LVEGTQGIGVVLAEtRQAAESVIDAFRGL 170
Cdd:TIGR01369 663 SIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEI-GYPVLVRpsYVLGGRAMEIVYNE-EELRRYLEEAVAVS 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 171 NAH-ILVQEYIAEAKGCDIRCLVVGNEVVAA--IERCAKAGdfrsnLHRGGVASI-------ATITPRERDIAIKAAqtL 240
Cdd:TIGR01369 741 PEHpVLIDKYLEDAVEVDVDAVSDGEEVLIPgiMEHIEEAG-----VHSGDSTCVlppqtlsAEIVDRIKDIVRKIA--K 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446607020 241 GLDVAG---VDILRAARGPLVMEVN--ASPGLEGIEKTTGVDIAGRMI 283
Cdd:TIGR01369 814 ELNVKGlmnIQFAVKDGEVYVIEVNprASRTVPFVSKATGVPLAKLAV 861
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
97-269 |
1.63e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 39.50 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 97 ARDKLRSLQLLARQGI------DLPITGIAHSPDDTsdLIKMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRG 169
Cdd:PRK14572 128 AMDKTRANQIFLQSGQkvapffELEKLKYLNSPRKT--LLKLESlGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446607020 170 LNAHILVQEYIAeakGCDIRCLVVGNEVVAAIERCAKAG----------DFRSNLHRGGVASIA------TITPRERDIA 233
Cdd:PRK14572 206 SDSKVMSQSFLS---GTEVSCGVLERYRGGKRNPIALPAteivpggeffDFESKYKQGGSEEITparisdQEMKRVQELA 282
|
170 180 190
....*....|....*....|....*....|....*..
gi 446607020 234 IKAAQTLGLD-VAGVDILRAARGPLVMEVNASPGLEG 269
Cdd:PRK14572 283 IRAHESLGCKgYSRTDFIIVDGEPHILETNTLPGMTE 319
|
|
| |
