|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-235 |
5.02e-135 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 379.80 E-value: 5.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVG 80
Cdd:PRK00748 1 MIIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 81 GGIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGA 160
Cdd:PRK00748 81 GGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLEHqgVTGVIVGKALYTGDISLPEA 235
Cdd:PRK00748 161 KAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGA--VEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
2-240 |
8.34e-128 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 361.66 E-value: 8.34e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 2 EVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGG 81
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 82 GIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGAA 161
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283834 162 AIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISLPEALRAIG 240
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALALAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
2-237 |
4.40e-122 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 347.16 E-value: 4.40e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 2 EVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGG 81
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 82 GIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPH-QIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGA 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISLPEALR 237
Cdd:cd04732 161 KAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
2-231 |
2.04e-107 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 309.79 E-value: 2.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 2 EVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 82 GIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQ-IMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGA 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQcIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDIS 231
Cdd:pfam00977 161 GEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
3-234 |
1.22e-101 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 295.26 E-value: 1.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 3 VIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGGG 82
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 83 IRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQF-PHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGAA 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948283834 162 AIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISLPE 234
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKL---GVYGVIVGKALYEGKITLEE 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-235 |
5.02e-135 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 379.80 E-value: 5.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVG 80
Cdd:PRK00748 1 MIIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 81 GGIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGA 160
Cdd:PRK00748 81 GGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVVGLDARDGKVATDGWLETSGVTAEDLAKRFEDAGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLEHqgVTGVIVGKALYTGDISLPEA 235
Cdd:PRK00748 161 KAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGA--VEGVIVGRALYEGKFDLAEA 233
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
2-240 |
8.34e-128 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 361.66 E-value: 8.34e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 2 EVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGG 81
Cdd:COG0106 1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 82 GIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGAA 161
Cdd:COG0106 81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERIVVGLDARDGKVATDGWQETSGVDLEELAKRFEDAGVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283834 162 AIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISLPEALRAIG 240
Cdd:COG0106 161 AILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLRALKEL---GVEGAIVGKALYEGKIDLEEALALAR 236
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
2-237 |
4.40e-122 |
|
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.
Pssm-ID: 240083 Cd Length: 234 Bit Score: 347.16 E-value: 4.40e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 2 EVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGG 81
Cdd:cd04732 1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 82 GIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPH-QIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGA 160
Cdd:cd04732 81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGeRIVVGLDAKDGKVATKGWLETSEVSLEELAKRFEELGV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISLPEALR 237
Cdd:cd04732 161 KAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKALKEL---GVAGVIVGKALYEGKITLEEALA 234
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
2-231 |
2.04e-107 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 309.79 E-value: 2.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 2 EVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGG 81
Cdd:pfam00977 1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 82 GIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQ-IMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGA 160
Cdd:pfam00977 81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQcIVVAIDARRGKVAINGWREDTGIDAVEWAKELEELGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDIS 231
Cdd:pfam00977 161 GEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTE---GVDGVIAGSALYEGEIT 228
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
3-234 |
1.22e-101 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 295.26 E-value: 1.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 3 VIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGGG 82
Cdd:TIGR00007 1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 83 IRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQF-PHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGAA 161
Cdd:TIGR00007 81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYgPERIVVSLDARGGEVAVKGWLEKSEVSLEELAKRLEELGLE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 948283834 162 AIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISLPE 234
Cdd:TIGR00007 161 GIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKL---GVYGVIVGKALYEGKITLEE 230
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
1-240 |
4.16e-81 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 243.66 E-value: 4.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVG 80
Cdd:PRK13585 3 FEVIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 81 GGIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQF-PHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELG 159
Cdd:PRK13585 83 GGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFgSERVMVSLDAKDGEVVIKGWTEKTGYTPVEAAKRFEELG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 160 AAAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTllsLEHQGVTGVIVGKALYTGDISLPEALRAI 239
Cdd:PRK13585 163 AGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRA---LKEAGAAGVVVGSALYKGKFTLEEAIEAV 239
|
.
gi 948283834 240 G 240
Cdd:PRK13585 240 K 240
|
|
| PRK14024 |
PRK14024 |
phosphoribosyl isomerase A; Provisional |
1-240 |
1.03e-56 |
|
phosphoribosyl isomerase A; Provisional
Pssm-ID: 237589 Cd Length: 241 Bit Score: 181.31 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDyAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAkAGRVVNLSAIEAITNAVSIPIEVG 80
Cdd:PRK14024 4 LTLLPAVDVVDGQAVRLVQGE-AGSETSYGSPLDAALAWQRDGAEWIHLVDLDAA-FGRGSNRELLAEVVGKLDVKVELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 81 GGIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQIMVGIDARNGLVAIRGWLETSQILAPQLAtQMQELGA 160
Cdd:PRK14024 82 GGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVGLDVRGHTLAARGWTRDGGDLWEVLE-RLDSAGC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLEHQGVTGVIVGKALYTGDISLPEALRAIG 240
Cdd:PRK14024 161 SRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRALAELVPLGVEGAIVGKALYAGAFTLPEALAVVR 240
|
|
| PRK04128 |
PRK04128 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-236 |
3.96e-51 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 167709 Cd Length: 228 Bit Score: 166.49 E-value: 3.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDYAQSQVYShNPVETAKMWADQgATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVG 80
Cdd:PRK04128 2 MRIYPAIDLMNGKAVRLYKGRKEEVKVYG-DPVEIALRFSEY-VDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 81 GGIRDRSSVIQLFSLGVQWAILGTVAVEQpDLVQGLCEQFpHQIMVGIDARNGLVAIRGWLETSQILaPQLATQMQELGA 160
Cdd:PRK04128 80 GGLRTYESIKDAYEIGVENVIIGTKAFDL-EFLEKVTSEF-EGITVSLDVKGGRIAVKGWLEESSIK-VEDAYEMLKNYV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948283834 161 AAIIYTDINRDGTLQG-PNLEALRGltsaiSIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISLPEAL 236
Cdd:PRK04128 157 NRFIYTSIERDGTLTGiEEIERFWG-----DEEFIYAGGVSSAEDVKKLAEI---GFSGVIIGKALYEGRISLEELL 225
|
|
| PRK13587 |
PRK13587 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
1-227 |
4.57e-47 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional
Pssm-ID: 172156 Cd Length: 234 Bit Score: 156.53 E-value: 4.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWAD-QGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEV 79
Cdd:PRK13587 2 IELWPAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 80 GGGIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELG 159
Cdd:PRK13587 82 GGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRIYLSVDAYGEDIKVNGWEEDTELNLFSFVRQLSDIP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 948283834 160 AAAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYT 227
Cdd:PRK13587 162 LGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASL---NVHAAIIGKAAHQ 226
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
3-235 |
3.31e-40 |
|
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240082 Cd Length: 243 Bit Score: 138.75 E-value: 3.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 3 VIPAIDLLEGRcvrLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGGG 82
Cdd:cd04731 3 IIPCLDVKDGR---VVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 83 IRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQ-IMVGIDA-RNGL----VAIRGWLETSQILAPQLATQMQ 156
Cdd:cd04731 80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQcVVVSIDAkRRGDggyeVYTHGGRKPTGLDAVEWAKEVE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948283834 157 ELGAAAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLlsLEHQGVTGVIVGKALYTGDISLPEA 235
Cdd:cd04731 160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEA--FEEGGADAALAASIFHFGEYTIAEL 236
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
2-237 |
5.65e-38 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 132.78 E-value: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 2 EVIPAIDLLEGRCVRLYKGD---YAQSQ---VYSHNPVETAKMWADQGATRLHLVDLDgAKAGRVVNLSAIEAITNAVSI 75
Cdd:cd04723 1 RIIPVIDLKDGVVVHGVGGDrdnYRPITsnlCSTSDPLDVARAYKELGFRGLYIADLD-AIMGRGDNDEAIRELAAAWPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 76 PIEVGGGIRDRSSVIQLFSLGVQWAILGTVAVE---QPDLVQGLCEQfphQIMVGIDARNGLVAIRGWLETSQILAPQLA 152
Cdd:cd04723 80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPsddDEDRLAALGEQ---RLVLSLDFRGGQLLKPTDFIGPEELLRRLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 153 TQMQElgaaaIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDISL 232
Cdd:cd04723 157 KWPEE-----LIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKL---GASGALVASALHDGGLTL 228
|
....*
gi 948283834 233 PEALR 237
Cdd:cd04723 229 EDVVR 233
|
|
| PRK14114 |
PRK14114 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-232 |
1.12e-36 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 172604 Cd Length: 241 Bit Score: 129.75 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSiPIEVG 80
Cdd:PRK14114 1 MLVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 81 GGIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLcEQFPHQIMVGIDARNGLVAIRGWLETSQILAPQLATQMQELGA 160
Cdd:PRK14114 80 GGIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFL-KEIDVEPVFSLDTRGGKVAFKGWLAEEEIDPVSLLKRLKEYGL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948283834 161 AAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLEHQG---VTGVIVGKALYTGDISL 232
Cdd:PRK14114 159 EEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQRVHRETnglLKGVIVGRAFLEGILTV 233
|
|
| hisF |
TIGR00735 |
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ... |
3-200 |
9.22e-35 |
|
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273241 Cd Length: 254 Bit Score: 125.17 E-value: 9.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 3 VIPAIDLLEGRCVrlyKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGGG 82
Cdd:TIGR00735 6 IIPCLDVRDGRVV---KGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 83 IRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQ-IMVGIDARNGLVAIRGWL--------ETSQILAPQLAT 153
Cdd:TIGR00735 83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQcIVVAIDAKRVYVNSYCWYevyiyggrESTGLDAVEWAK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 948283834 154 QMQELGAAAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVG 200
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAG 209
|
|
| HisF |
COG0107 |
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ... |
3-206 |
1.35e-33 |
|
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439877 Cd Length: 251 Bit Score: 122.05 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 3 VIPAIDLLEGRCVrlyKGDYAQSQVYSHNPVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNAVSIPIEVGGG 82
Cdd:COG0107 5 IIPCLDVKDGRVV---KGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 83 IRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFPHQ-IMVGIDAR---NG--LVAIRGWLETSQILAPQLATQMQ 156
Cdd:COG0107 82 IRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQcIVVAIDAKrvpDGgwEVYTHGGRKPTGLDAVEWAKEAE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 948283834 157 ELGAAAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLL 206
Cdd:COG0107 162 ELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFV 211
|
|
| PRK13586 |
PRK13586 |
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ... |
1-230 |
6.85e-25 |
|
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;
Pssm-ID: 237439 Cd Length: 232 Bit Score: 98.66 E-value: 6.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 1 MEVIPAIDLLEGRCVRLYKGDYAQSQVYShNPVETAKMWADQGATRLHLVDLDGAKaGRVVNLSAIEAITNAVSIPIEVG 80
Cdd:PRK13586 2 SKIIPSIDISLGKAVKRIRGVKGTGLILG-NPIEIASKLYNEGYTRIHVVDLDAAE-GVGNNEMYIKEISKIGFDWIQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 81 GGIRDRSSVIQLFSLGVQWAILGTVAVEQPDLVQGLCEQFP-HQIMVGID-ARNGLVAIRGWLETSQILAPQLaTQMQEL 158
Cdd:PRK13586 80 GGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGsNRVLVSIDyDNTKRVLIRGWKEKSMEVIDGI-KKVNEL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948283834 159 GAAAIIYTDINRDGTLQGPNLEALRgltSAISIPVIA--SGGVGSVTDLLTLLSLehqGVTGVIVGKALYTGDI 230
Cdd:PRK13586 159 ELLGIIFTYISNEGTTKGIDYNVKD---YARLIRGLKeyAGGVSSDADLEYLKNV---GFDYIIVGMAFYLGKL 226
|
|
| PLN02617 |
PLN02617 |
imidazole glycerol phosphate synthase hisHF |
32-202 |
1.04e-08 |
|
imidazole glycerol phosphate synthase hisHF
Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 55.10 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 32 PVETAKMWADQGATRLHLVDLDGAKAGRVVNLSAIEAITNA---VSIPIEVGGGIRD-------------------RSSV 89
Cdd:PLN02617 269 PVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEVLRRAsenVFVPLTVGGGIRDftdangryysslevaseyfRSGA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 90 --IQLFSLGVQWA--------ILGTVAVEQPDLVQGLceqfpHQIMVGIDARNGLVA----------------------- 136
Cdd:PLN02617 349 dkISIGSDAVYAAeeyiasgvKTGKTSIEQISRVYGN-----QAVVVSIDPRRVYVKdpsdvpfktvkvtnpgpngeeya 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948283834 137 -----IRGWLETSQILAPQLATQMQELGAAAIIYTDINRDGTLQGPNLEALRGLTSAISIPVIASGGVGSV 202
Cdd:PLN02617 424 wyqctVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTP 494
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
137-226 |
1.40e-05 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 45.47 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 137 IR-GWLETSqILAPQLATQMQELGAAAII---------YTdinrdgtlqGP-NLEALRGLTSAISIPVIASGGVGSVTDL 205
Cdd:COG0042 137 IRlGWDDDD-ENALEFARIAEDAGAAALTvhgrtreqrYK---------GPaDWDAIARVKEAVSIPVIGNGDIFSPEDA 206
|
90 100
....*....|....*....|.
gi 948283834 206 LTLlsLEHQGVTGVIVGKALY 226
Cdd:COG0042 207 KRM--LEETGCDGVMIGRGAL 225
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
137-226 |
2.41e-05 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 44.41 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 137 IR-GWleTSQILAPQLATQMQELGAAAII---------YTdinrdgtlqGP-NLEALRGLTSAISIPVIASGGVGSVTDL 205
Cdd:cd02801 130 IRlGW--DDEEETLELAKALEDAGASALTvhgrtreqrYS---------GPaDWDYIAEIKEAVSIPVIANGDIFSLEDA 198
|
90 100
....*....|....*....|.
gi 948283834 206 LTLlsLEHQGVTGVIVGKALY 226
Cdd:cd02801 199 LRC--LEQTGVDGVMIGRGAL 217
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
135-257 |
2.21e-04 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 41.93 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 135 VAIR-GWLETSQiLAPQLATQMQELGAAAIIytdI-------NRDGTLqgpNLEALRGLTSAISIPVIASGGVGSVTDLL 206
Cdd:pfam01207 127 VKIRiGWDDSHE-NAVEIAKIVEDAGAQALT---VhgrtraqNYEGTA---DWDAIKQVKQAVSIPVIANGDITDPEDAQ 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 948283834 207 TLlsLEHQGVTGVIVGKALYtGDISLPEALRAIGPGRIQDIPPTLDFSSFA 257
Cdd:pfam01207 200 RC--LAYTGADGVMIGRGAL-GNPWLFAEQHTVKTGEFGPSPPLAEEAEKV 247
|
|
| Peptidase_U32 |
pfam01136 |
Peptidase family U32; |
30-79 |
5.34e-04 |
|
Peptidase family U32;
Pssm-ID: 426072 Cd Length: 233 Bit Score: 40.26 E-value: 5.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 948283834 30 HNPvETAKMWADQGATRLHLvdldgakaGRVVNLSAIEAITNAVSIPIEV 79
Cdd:pfam01136 48 TNS-EAARFWKELGASRVVL--------ARELSLEEIKEIKENTDVELEV 88
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
32-222 |
1.25e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 38.72 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 32 PVETAKMWADQGATRLHLVDLDGAKAGRV-VNLSAIEAITNAVSIPIEVGGGIRDRS-----SVIQLFSLGVQWAILGTV 105
Cdd:cd04722 14 PVELAKAAAEAGADAIIVGTRSSDPEEAEtDDKEVLKEVAAETDLPLGVQLAINDAAaavdiAAAAARAAGADGVEIHGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 106 ----AVEQPDLVQGLCEQFPHQ-IMVGIDARNGLVAIrgwletsqilapqlatQMQELGAAAIIYTDINRDGTLQGPNLE 180
Cdd:cd04722 94 vgylAREDLELIRELREAVPDVkVVVKLSPTGELAAA----------------AAEEAGVDEVGLGNGGGGGGGRDAVPI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 948283834 181 ALRGLT---SAISIPVIASGGVGSVTDLLTLLsleHQGVTGVIVG 222
Cdd:cd04722 158 ADLLLIlakRGSKVPVIAGGGINDPEDAAEAL---ALGADGVIVG 199
|
|
| RlhA |
COG0826 |
23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family ... |
30-79 |
2.80e-03 |
|
23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family [Translation, ribosomal structure and biogenesis]; 23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440588 Cd Length: 311 Bit Score: 38.20 E-value: 2.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 948283834 30 HNPvETAKMWADQGATRLHLvdldgakaGRVVNLSAIEAITNAVSIPIEV 79
Cdd:COG0826 122 TNS-EAVKFLKELGASRVVL--------ARELSLEEIKEIREKTDVELEV 162
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
174-237 |
3.42e-03 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 37.69 E-value: 3.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 948283834 174 LQGPNLEALRGLTSAISIPVIASGGV--GSVTDLLtllsleHQGVTGVIVGKALYTGDISLPEALR 237
Cdd:PRK07695 133 VPARGLEELSDIARALSIPVIAIGGItpENTRDVL------AAGVSGIAVMSGIFSSANPYSKAKR 192
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
144-222 |
7.85e-03 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 36.69 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948283834 144 SQILAPQLATQMQELGAAAIIYTdiNRD-----GTLQGPNLEALRGLTSAISIPVIASGGVGSVTDLLTLLSLehqGVTG 218
Cdd:cd04730 107 PTVTSVEEARKAEAAGADALVAQ--GAEagghrGTFDIGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALAL---GADG 181
|
....
gi 948283834 219 VIVG 222
Cdd:cd04730 182 VQMG 185
|
|
| |
