|
Name |
Accession |
Description |
Interval |
E-value |
| PanC |
COG0414 |
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ... |
1-280 |
0e+00 |
|
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440183 [Multi-domain] Cd Length: 280 Bit Score: 540.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:COG0414 1 MKIIRTIAELRAALAAWRAAGKRIGLVPTMGALHEGHLSLVRRARAEADVVVVSIFVNPLQFGPNEDLDRYPRTLEADLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYPPDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRRM 160
Cdd:COG0414 81 LLEAAGVDLVFAPSVEEMYPEGFSTRVDVGGLSEVLEGASRPGHFDGVATVVTKLFNIVQPDVAYFGEKDYQQLAVIRRM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 161 VRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDKVKID 240
Cdd:COG0414 161 VRDLNLPVEIVGVPTVREADGLALSSRNVYLSPEERAAAPALYRALQAAAEAIAAGERDAAALLAAARAALAAAPFVRLD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
2EJC_A 241 YVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDNTILG 280
Cdd:COG0414 241 YVEIVDAETLEPVEEIDGPALLLVAARLGKTRLIDNIVLN 280
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
2-278 |
0e+00 |
|
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.
Pssm-ID: 460595 [Multi-domain] Cd Length: 277 Bit Score: 523.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 2 RIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRKL 81
Cdd:pfam02569 1 KIIRTIAELRAWLRAWRRAGKTIGLVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDLDAYPRTLEADLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 82 LEKENVDCIFHPSVEEMYPPDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRRMV 161
Cdd:pfam02569 81 LEAAGVDLVFAPSVEEMYPEGFSTTVDVPGLSEVLEGASRPGHFRGVATVVTKLFNIVQPDRAYFGEKDYQQLAVIRRMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 162 RDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNgERDAEKIKEEMIKHLSRFDKVKIDY 241
Cdd:pfam02569 161 RDLNLPVEIVGCPTVREADGLALSSRNVYLSPEERAAAPVLYRALQAAAEAIRA-ERDAAALLAAARERLAAAGFARVDY 239
|
250 260 270
....*....|....*....|....*....|....*...
2EJC_A 242 VEIVDEETL-EPVEKIDRKVIVAVAAWVGNARLIDNTI 278
Cdd:pfam02569 240 VEIVDADTLeEPLEDIAGPAVLLVAARLGKTRLIDNII 277
|
|
| PanC |
cd00560 |
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate ... |
1-276 |
0e+00 |
|
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate synthase, catalyzes the formation of pantothenate from pantoate and alanine. PanC belongs to a large superfamily of nucleotidyltransferases that includes , ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 185673 [Multi-domain] Cd Length: 277 Bit Score: 508.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:cd00560 1 MRIITTIAELRAWLRNWRAQGKTIGFVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPLQFGPNEDLDRYPRTLEADLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYP-PDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRR 159
Cdd:cd00560 81 LLEEAGVDLLFAPSVEEMYPeGLFSTFVDVGPLSEVLEGASRPGHFRGVATVVAKLFNLVQPDRAYFGEKDAQQLAVIRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 160 MVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDkVKI 239
Cdd:cd00560 161 MVRDLNLPVEIVGCPTVREEDGLALSSRNVYLSAEERKEALALYRALKAAAEAIAAGERDAEDIIAAARDVLEAAG-FRV 239
|
250 260 270
....*....|....*....|....*....|....*..
2EJC_A 240 DYVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDN 276
Cdd:cd00560 240 DYLEIVDPETLEPVEEIDKPAVILVAARVGKTRLIDN 276
|
|
| PRK13477 |
PRK13477 |
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase; |
1-279 |
1.62e-146 |
|
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
Pssm-ID: 237393 [Multi-domain] Cd Length: 512 Bit Score: 420.44 E-value: 1.62e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKkkTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:PRK13477 1 MRILRTVAGLRAWLRQQRSE--TIGFVPTMGALHQGHLSLIRRARQENDVVLVSIFVNPLQFGPNEDLERYPRTLEADRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYPPDFS--TYVEETK-LSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVL 157
Cdd:PRK13477 79 LCESAGVDAIFAPSPEELYPGGAKsiTQVQPPSeLTSHLCGASRPGHFDGVATVVTRLLNLVQPKRAYFGEKDWQQLAII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 158 RRMVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDKV 237
Cdd:PRK13477 159 RRLVADLNLPVTIVGCPTVREADGLALSSRNQYLSAEERQQAAALYRALQAAKKAFQAGKRINLNLLAAVQEELLSEPGL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
2EJC_A 238 KIDYVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDNTIL 279
Cdd:PRK13477 239 EVEYLELVDPQTLQPLEQIENIGLLAIAVRCGSTRLIDNVFL 280
|
|
| panC |
TIGR00018 |
pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme ... |
1-279 |
2.40e-130 |
|
pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme of pantothenate biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 272857 [Multi-domain] Cd Length: 282 Bit Score: 371.02 E-value: 2.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:TIGR00018 1 MRIIETIPLLRQYIRQLRMEGKTVGFVPTMGNLHDGHMSLIDRAVAENDVVVVSIFVNPMQFGPNEDLEAYPRTLEEDCA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYP---PDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVL 157
Cdd:TIGR00018 81 LLEKLGVDVVFAPSVHEMYPngtEQHTTVDVPLGLSEVLEGASRPGHFRGVATIVTKLFNLVQPDVAYFGEKDAQQLAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 158 RRMVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDkV 237
Cdd:TIGR00018 161 RKLVADLFLDIEIVPVPIVREEDGLALSSRNVYLTAEQRKIAPGLYRALQAIAQAIQAGERDLDAVITIAGDILDTKS-F 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
2EJC_A 238 KIDYVEIVDEETLEPVEKID-RKVIVAVAAWVGNARLIDNTIL 279
Cdd:TIGR00018 240 RIDYVQLRDADTLEPVSETEpTSAVILVAAYVGDARLIDNIVV 282
|
|
| PGA_cap |
smart00854 |
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ... |
38-95 |
1.42e-03 |
|
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.
Pssm-ID: 214858 [Multi-domain] Cd Length: 239 Bit Score: 39.11 E-value: 1.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
2EJC_A 38 LSLVRRARAENDVVVVSIfvnptQFGPNedYERYPRDFERD--RKLLEkENVDCIF--HPSV 95
Cdd:smart00854 163 LADIARARKEADVVIVSL-----HWGVE--YQYEPTPEQRElaHALID-AGADVVIghHPHV 216
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PanC |
COG0414 |
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ... |
1-280 |
0e+00 |
|
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440183 [Multi-domain] Cd Length: 280 Bit Score: 540.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:COG0414 1 MKIIRTIAELRAALAAWRAAGKRIGLVPTMGALHEGHLSLVRRARAEADVVVVSIFVNPLQFGPNEDLDRYPRTLEADLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYPPDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRRM 160
Cdd:COG0414 81 LLEAAGVDLVFAPSVEEMYPEGFSTRVDVGGLSEVLEGASRPGHFDGVATVVTKLFNIVQPDVAYFGEKDYQQLAVIRRM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 161 VRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDKVKID 240
Cdd:COG0414 161 VRDLNLPVEIVGVPTVREADGLALSSRNVYLSPEERAAAPALYRALQAAAEAIAAGERDAAALLAAARAALAAAPFVRLD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
2EJC_A 241 YVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDNTILG 280
Cdd:COG0414 241 YVEIVDAETLEPVEEIDGPALLLVAARLGKTRLIDNIVLN 280
|
|
| Pantoate_ligase |
pfam02569 |
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ... |
2-278 |
0e+00 |
|
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.
Pssm-ID: 460595 [Multi-domain] Cd Length: 277 Bit Score: 523.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 2 RIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRKL 81
Cdd:pfam02569 1 KIIRTIAELRAWLRAWRRAGKTIGLVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDLDAYPRTLEADLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 82 LEKENVDCIFHPSVEEMYPPDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRRMV 161
Cdd:pfam02569 81 LEAAGVDLVFAPSVEEMYPEGFSTTVDVPGLSEVLEGASRPGHFRGVATVVTKLFNIVQPDRAYFGEKDYQQLAVIRRMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 162 RDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNgERDAEKIKEEMIKHLSRFDKVKIDY 241
Cdd:pfam02569 161 RDLNLPVEIVGCPTVREADGLALSSRNVYLSPEERAAAPVLYRALQAAAEAIRA-ERDAAALLAAARERLAAAGFARVDY 239
|
250 260 270
....*....|....*....|....*....|....*...
2EJC_A 242 VEIVDEETL-EPVEKIDRKVIVAVAAWVGNARLIDNTI 278
Cdd:pfam02569 240 VEIVDADTLeEPLEDIAGPAVLLVAARLGKTRLIDNII 277
|
|
| PanC |
cd00560 |
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate ... |
1-276 |
0e+00 |
|
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate synthase, catalyzes the formation of pantothenate from pantoate and alanine. PanC belongs to a large superfamily of nucleotidyltransferases that includes , ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 185673 [Multi-domain] Cd Length: 277 Bit Score: 508.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:cd00560 1 MRIITTIAELRAWLRNWRAQGKTIGFVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPLQFGPNEDLDRYPRTLEADLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYP-PDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVLRR 159
Cdd:cd00560 81 LLEEAGVDLLFAPSVEEMYPeGLFSTFVDVGPLSEVLEGASRPGHFRGVATVVAKLFNLVQPDRAYFGEKDAQQLAVIRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 160 MVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDkVKI 239
Cdd:cd00560 161 MVRDLNLPVEIVGCPTVREEDGLALSSRNVYLSAEERKEALALYRALKAAAEAIAAGERDAEDIIAAARDVLEAAG-FRV 239
|
250 260 270
....*....|....*....|....*....|....*..
2EJC_A 240 DYVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDN 276
Cdd:cd00560 240 DYLEIVDPETLEPVEEIDKPAVILVAARVGKTRLIDN 276
|
|
| PRK13477 |
PRK13477 |
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase; |
1-279 |
1.62e-146 |
|
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
Pssm-ID: 237393 [Multi-domain] Cd Length: 512 Bit Score: 420.44 E-value: 1.62e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKkkTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:PRK13477 1 MRILRTVAGLRAWLRQQRSE--TIGFVPTMGALHQGHLSLIRRARQENDVVLVSIFVNPLQFGPNEDLERYPRTLEADRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYPPDFS--TYVEETK-LSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVL 157
Cdd:PRK13477 79 LCESAGVDAIFAPSPEELYPGGAKsiTQVQPPSeLTSHLCGASRPGHFDGVATVVTRLLNLVQPKRAYFGEKDWQQLAII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 158 RRMVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDKV 237
Cdd:PRK13477 159 RRLVADLNLPVTIVGCPTVREADGLALSSRNQYLSAEERQQAAALYRALQAAKKAFQAGKRINLNLLAAVQEELLSEPGL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
2EJC_A 238 KIDYVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDNTIL 279
Cdd:PRK13477 239 EVEYLELVDPQTLQPLEQIENIGLLAIAVRCGSTRLIDNVFL 280
|
|
| PLN02660 |
PLN02660 |
pantoate--beta-alanine ligase |
3-279 |
7.20e-142 |
|
pantoate--beta-alanine ligase
Pssm-ID: 178266 [Multi-domain] Cd Length: 284 Bit Score: 400.19 E-value: 7.20e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 3 IIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRKLL 82
Cdd:PLN02660 2 VIRDKAAMRAWSRAQRAQGKRIALVPTMGYLHEGHLSLVRAARARADVVVVSIYVNPGQFAPGEDLDTYPRDFDGDLRKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 83 EKENVDCIFHP-------SVEEMYPPDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFR 155
Cdd:PLN02660 82 AALGVDAVFNPhdlyvyvSCLEEGGAGHETWVRVERLEKGLCGKSRPVFFRGVATIVTKLFNIVEPDVAVFGKKDYQQWR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 156 VLRRMVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRfD 235
Cdd:PLN02660 162 VIRRMVRDLDFDIEVVGSPIVREADGLAMSSRNVRLSAEEREKALSISRSLARAEELVEEGETDADELKEQVRQAIAE-A 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
2EJC_A 236 KVKIDYVEIVDEETLEPVEKIDRKVIVAVAAWVGNARLIDNTIL 279
Cdd:PLN02660 241 GGEVDYVEIVDQETLQPVEEIKSPVVIAVAAWFGSVRLIDNIEL 284
|
|
| panC |
TIGR00018 |
pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme ... |
1-279 |
2.40e-130 |
|
pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme of pantothenate biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 272857 [Multi-domain] Cd Length: 282 Bit Score: 371.02 E-value: 2.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 1 MRIIETIEEMKKFSEEMREKKKTIGFVPTMGYLHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDYERYPRDFERDRK 80
Cdd:TIGR00018 1 MRIIETIPLLRQYIRQLRMEGKTVGFVPTMGNLHDGHMSLIDRAVAENDVVVVSIFVNPMQFGPNEDLEAYPRTLEEDCA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 81 LLEKENVDCIFHPSVEEMYP---PDFSTYVEETKLSKHLCGRSRPGHFRGVCTVVTKLFNIVKPHRAYFGQKDAQQFRVL 157
Cdd:TIGR00018 81 LLEKLGVDVVFAPSVHEMYPngtEQHTTVDVPLGLSEVLEGASRPGHFRGVATIVTKLFNLVQPDVAYFGEKDAQQLAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 158 RRMVRDLNMDVEMIECPIVREPDGLAMSSRNVYLSPEERQQALSLYQSLKIAENLYLNGERDAEKIKEEMIKHLSRFDkV 237
Cdd:TIGR00018 161 RKLVADLFLDIEIVPVPIVREEDGLALSSRNVYLTAEQRKIAPGLYRALQAIAQAIQAGERDLDAVITIAGDILDTKS-F 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
2EJC_A 238 KIDYVEIVDEETLEPVEKID-RKVIVAVAAWVGNARLIDNTIL 279
Cdd:TIGR00018 240 RIDYVQLRDADTLEPVSETEpTSAVILVAAYVGDARLIDNIVV 282
|
|
| cytidylyltransferase_like |
cd02039 |
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
24-191 |
5.81e-07 |
|
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.
Pssm-ID: 185678 [Multi-domain] Cd Length: 143 Bit Score: 47.82 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 24 IGFVPTMGY-LHEGHLSLVRRARAEN-DVVVVSIFVNPTQFGPNEDYERYPRDFERDRKLLEK-ENVDCIFHPSVEEMYP 100
Cdd:cd02039 1 VGIIIGRFEpFHLGHLKLIKEALEEAlDEVIIIIVSNPPKKKRNKDPFSLHERVEMLKEILKDrLKVVPVDFPEVKILLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 101 PDFstyveetklskhlcgrsrpghfrgvctvVTKLFNIVKPHRAYFGQKDAQQF-RVLRRMVRDLNMDVEMIECPIVRep 179
Cdd:cd02039 81 VVF----------------------------ILKILLKVGPDKVVVGEDFAFGKnASYNKDLKELFLDIEIVEVPRVR-- 130
|
170
....*....|..
2EJC_A 180 DGLAMSSRNVYL 191
Cdd:cd02039 131 DGKKISSTLIRE 142
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
26-88 |
1.17e-06 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 44.99 E-value: 1.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
2EJC_A 26 FVPTMGYLHEGHLSLVRRARAENDVVVVsiFVNPTQFGPNEDYERYPRDFERdRKLLEKENVD 88
Cdd:TIGR00125 4 FVGTFDPFHLGHLDLLERAKELFDELIV--GVGSDQFVNPLKGEPVFSLEER-LEMLKALKYV 63
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
26-78 |
1.42e-05 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 43.30 E-value: 1.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
2EJC_A 26 FVPTM-GYLHEGHLSLVRRARAENDVVVVSIFVNPTQFgPNEDYERYPRDFERD 78
Cdd:cd02156 3 RFPGEpGYLHIGHAKLICRAKGIADQCVVRIDDNPPVK-VWQDPHELEERKESI 55
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
4-93 |
4.42e-04 |
|
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and metabolism, General function prediction only]; Histidinol phosphatase or related hydrolase of the PHP family is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 440997 [Multi-domain] Cd Length: 232 Bit Score: 40.52 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 4 IETIEEMKKFSEEMR-----EkkktigfvptMGYLHEGHLSLVRRARAENDVVVVSIfvnptQFGPNEDYERYprdFERD 78
Cdd:COG1387 57 LEEIEELNEKYPDIKilkgiE----------VDILPDGSLDYPDELLAPLDYVIGSV-----HSILEEDYEEY---TERL 118
|
90
....*....|....*
2EJC_A 79 RKLLEKENVDCIFHP 93
Cdd:COG1387 119 LKAIENPLVDILGHP 133
|
|
| CapA |
COG2843 |
Poly-gamma-glutamate biosynthesis protein CapA/YwtB (capsule formation), metallophosphatase ... |
40-95 |
4.94e-04 |
|
Poly-gamma-glutamate biosynthesis protein CapA/YwtB (capsule formation), metallophosphatase superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442091 [Multi-domain] Cd Length: 310 Bit Score: 41.05 E-value: 4.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
2EJC_A 40 LVRRARAENDVVVVSIfvnptQFGPNedYERYPRDFERD--RKLLEkENVDCIF--HPSV 95
Cdd:COG2843 171 DIAAARAGADLVIVSL-----HWGVE--YEREPNPEQRElaRALID-AGADLVIghHPHV 222
|
|
| PGA_cap |
smart00854 |
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate ... |
38-95 |
1.42e-03 |
|
Bacterial capsule synthesis protein PGA_cap; This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.
Pssm-ID: 214858 [Multi-domain] Cd Length: 239 Bit Score: 39.11 E-value: 1.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
2EJC_A 38 LSLVRRARAENDVVVVSIfvnptQFGPNedYERYPRDFERD--RKLLEkENVDCIF--HPSV 95
Cdd:smart00854 163 LADIARARKEADVVIVSL-----HWGVE--YQYEPTPEQRElaHALID-AGADVVIghHPHV 216
|
|
| |
