|
Name |
Accession |
Description |
Interval |
E-value |
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
20-217 |
7.27e-94 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 272.68 E-value: 7.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLASGLGSLLQSMLELLDAEK--VQIVAVGSDK-DCPALERAQNLNIPTFRVPFDAVAkkDREGWDIRVLEAVNSF 96
Cdd:COG0299 2 KRIAVLISGRGSNLQALIDAIEAGDlpAEIVLVISNRpDAYGLERARAAGIPTFVLDHKDFP--SREAFDAALLEALDAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 97 SPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVED 176
Cdd:COG0299 80 GPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524658804 177 DDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRKAYLK 217
Cdd:COG0299 160 DDTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLD 200
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
21-202 |
2.87e-80 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 237.67 E-value: 2.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 21 RIVVLASGLGSLLQSmleLLDAEK-----VQIVAVGSDK-DCPALERAQNLNIPTFRVPFdaVAKKDREGWDIRVLEAVN 94
Cdd:cd08645 1 RIAVLASGSGSNLQA---LIDAIKsgklnAEIVLVISNNpDAYGLERAKKAGIPTFVINR--KDFPSREEFDEALLELLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 95 SFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAV 174
Cdd:cd08645 76 EYKVDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPV 155
|
170 180
....*....|....*....|....*...
gi 2524658804 175 EDDDTVETLHERIKVVERRLLVDVLHSI 202
Cdd:cd08645 156 LPGDTPETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
20-207 |
2.23e-69 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 210.31 E-value: 2.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLASGLGSLLQSMLELLDAEKV--QIVAVGSDK-DCPALERAQNLNIPTF---RVPFDAvakkdREGWDIRVLEAV 93
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIpaSVVLVISNKpDAYGLERAAQAGIPTFvlsLKDFPS-----REAFDQAIIEEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 94 NSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVA 173
Cdd:TIGR00639 76 RAHEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVP 155
|
170 180 190
....*....|....*....|....*....|....
gi 2524658804 174 VEDDDTVETLHERIKVVERRLLVDVLHSIADHGI 207
Cdd:TIGR00639 156 ILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGRL 189
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
20-199 |
1.74e-46 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 151.68 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLASGLGSLLQsmlELLDAEK-----VQIVAVGSDKDCPA-LERAQNLNIPTFRV---PFDAVAKKDREgwdirVL 90
Cdd:pfam00551 1 MKIAVLISGTGSNLQ---ALIDALRkggqdADVVLVISNKDKAAgLGRAEQAGIPTFVFehkGLTPRSLFDQE-----LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 91 EAVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQ 170
Cdd:pfam00551 73 DALRALAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQK 152
|
170 180
....*....|....*....|....*....
gi 2524658804 171 PVAVEDDDTVETLHERIKVVERRLLVDVL 199
Cdd:pfam00551 153 AVPILPDDTAETLYNRVADLEHKALPRVL 181
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
21-208 |
3.81e-29 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 107.86 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 21 RIVVLASGLGSLLQSMLELLDAEKV--QIVAVGSDK-DCPALERAQNLNIPTFRVPfdaVAKKDREGWDI-RVLEAVNSF 96
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVngDVVVVVTNKpGCGGAEYARENGIPVLVYP---KTKGEPDGLSPdELVDALRGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 97 SPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGA--------RAVpdaLDYGVKVTGTTVHIVDNGVDTGPILA 168
Cdd:PLN02331 78 GVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKgyygikvhKAV---IASGARYSGPTVHFVDEHYDTGRILA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524658804 169 QQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIADHGIE 208
Cdd:PLN02331 155 QRVVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
20-217 |
7.27e-94 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 272.68 E-value: 7.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLASGLGSLLQSMLELLDAEK--VQIVAVGSDK-DCPALERAQNLNIPTFRVPFDAVAkkDREGWDIRVLEAVNSF 96
Cdd:COG0299 2 KRIAVLISGRGSNLQALIDAIEAGDlpAEIVLVISNRpDAYGLERARAAGIPTFVLDHKDFP--SREAFDAALLEALDAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 97 SPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVED 176
Cdd:COG0299 80 GPDLVVLAGFMRILTPEFVRAFPGRIINIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2524658804 177 DDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRKAYLK 217
Cdd:COG0299 160 DDTEETLAARILEQEHRLYPEAIRLLAEGRLTLDGRRVRLD 200
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
21-202 |
2.87e-80 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 237.67 E-value: 2.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 21 RIVVLASGLGSLLQSmleLLDAEK-----VQIVAVGSDK-DCPALERAQNLNIPTFRVPFdaVAKKDREGWDIRVLEAVN 94
Cdd:cd08645 1 RIAVLASGSGSNLQA---LIDAIKsgklnAEIVLVISNNpDAYGLERAKKAGIPTFVINR--KDFPSREEFDEALLELLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 95 SFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAV 174
Cdd:cd08645 76 EYKVDLIVLAGFMRILSPEFLEAFPGRIINIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPV 155
|
170 180
....*....|....*....|....*...
gi 2524658804 175 EDDDTVETLHERIKVVERRLLVDVLHSI 202
Cdd:cd08645 156 LPGDTPETLAERIHALEHRLYPEAIKLL 183
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
20-207 |
2.23e-69 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 210.31 E-value: 2.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLASGLGSLLQSMLELLDAEKV--QIVAVGSDK-DCPALERAQNLNIPTF---RVPFDAvakkdREGWDIRVLEAV 93
Cdd:TIGR00639 1 KRIVVLISGNGSNLQAIIDACKEGKIpaSVVLVISNKpDAYGLERAAQAGIPTFvlsLKDFPS-----REAFDQAIIEEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 94 NSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVA 173
Cdd:TIGR00639 76 RAHEVDLVVLAGFMRILGPTFLSRFAGRILNIHPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVP 155
|
170 180 190
....*....|....*....|....*....|....
gi 2524658804 174 VEDDDTVETLHERIKVVERRLLVDVLHSIADHGI 207
Cdd:TIGR00639 156 ILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGRL 189
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
20-199 |
1.74e-46 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 151.68 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLASGLGSLLQsmlELLDAEK-----VQIVAVGSDKDCPA-LERAQNLNIPTFRV---PFDAVAKKDREgwdirVL 90
Cdd:pfam00551 1 MKIAVLISGTGSNLQ---ALIDALRkggqdADVVLVISNKDKAAgLGRAEQAGIPTFVFehkGLTPRSLFDQE-----LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 91 EAVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQ 170
Cdd:pfam00551 73 DALRALAADVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQK 152
|
170 180
....*....|....*....|....*....
gi 2524658804 171 PVAVEDDDTVETLHERIKVVERRLLVDVL 199
Cdd:pfam00551 153 AVPILPDDTAETLYNRVADLEHKALPRVL 181
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
22-199 |
7.60e-39 |
|
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.
Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 132.03 E-value: 7.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 22 IVVLASGlgSLLQSMLE-LLDAEKVQIVAVGSDKDcPALERAQNLNIPTFRVPFdavakKDREGWDIRVLEAVNSFSPDI 100
Cdd:cd08369 1 IVILGSG--NIGQRVLKaLLSKEGHEIVGVVTHPD-SPRGTAQLSLELVGGKVY-----LDSNINTPELLELLKEFAPDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 101 VVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTV 180
Cdd:cd08369 73 IVSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTA 152
|
170
....*....|....*....
gi 2524658804 181 ETLHERIKVVERRLLVDVL 199
Cdd:cd08369 153 GTLYQRLIELGPKLLKEAL 171
|
|
| FMT_core_Formyl-FH4-Hydrolase_C |
cd08648 |
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; ... |
21-213 |
3.89e-31 |
|
Formyltetrahydrofolate deformylase (Formyl-FH4 hydrolase), C-terminal hydrolase domain; Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Formate is the substrate of phosphoribosylglycinamide transformylase for step three of de novo purine nucleotide synthesis. Formyl-FH4 hydrolase has been proposed to regulate the balance of FH4 and C1-FH4 in the cell. The enzyme uses methionine and glycine to sense the pools of C1-FH4 and FH4, respectively. This domain belongs to the formyltransferase (FMT) domain superfamily. Members of this family have an N-terminal ACT domain, which is commonly involved in specifically bind an amino acid or other small ligand leading to regulation of the enzyme. The N-terminal of this protein family may be responsible for the binding of the regulators methionine and glycine.
Pssm-ID: 187717 [Multi-domain] Cd Length: 196 Bit Score: 112.66 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 21 RIVVLASGLGSLLQSML------ELldaeKVQIVAVGSDKdcPALER-AQNLNIPTFRVPfdaVAKKDREGWDIRVLEAV 93
Cdd:cd08648 2 RVAIFVSKEDHCLYDLLhrwregEL----PCEIPLVISNH--PDLRPlAERFGIPFHHIP---VTKDTKAEAEAEQLELL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 94 NSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVA 173
Cdd:cd08648 73 EEYGVDLVVLARYMQILSPDFVERYPNRIINIHHSFLPAFKGAKPYHQAFERGVKLIGATAHYVTEELDEGPIIEQDVER 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524658804 174 VEDDDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRK 213
Cdd:cd08648 153 VSHRDSVEDLVRKGRDIEKQVLARAVKWHLEDRVLVYGNK 192
|
|
| PurU |
COG0788 |
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate ... |
14-213 |
2.80e-29 |
|
Formyltetrahydrofolate hydrolase [Nucleotide transport and metabolism]; Formyltetrahydrofolate hydrolase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440551 [Multi-domain] Cd Length: 282 Bit Score: 110.14 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 14 NSSSKQLRIVVLASG----LGSLL--QSMLELldaeKVQIVAV-GSDKDCPALerAQNLNIPTFRVPFDAVAKKDREGwd 86
Cdd:COG0788 81 HDSDRRKRVAILVSKedhcLNDLLyrWRSGEL----PAEIPAViSNHPDLRPL--AEWFGIPFHHIPVTKETKAEAEA-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 87 iRVLEAVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPI 166
Cdd:COG0788 153 -RLLELLEEYDIDLVVLARYMQILSPDFCARLPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPI 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2524658804 167 LAQQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRK 213
Cdd:COG0788 232 IEQDVERVDHRDTPEDLVRKGRDVEKRVLARAVRWHLEDRVLVNGNK 278
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
21-208 |
3.81e-29 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 107.86 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 21 RIVVLASGLGSLLQSMLELLDAEKV--QIVAVGSDK-DCPALERAQNLNIPTFRVPfdaVAKKDREGWDI-RVLEAVNSF 96
Cdd:PLN02331 1 KLAVFVSGGGSNFRAIHDACLDGRVngDVVVVVTNKpGCGGAEYARENGIPVLVYP---KTKGEPDGLSPdELVDALRGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 97 SPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGA--------RAVpdaLDYGVKVTGTTVHIVDNGVDTGPILA 168
Cdd:PLN02331 78 GVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGKgyygikvhKAV---IASGARYSGPTVHFVDEHYDTGRILA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2524658804 169 QQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIADHGIE 208
Cdd:PLN02331 155 QRVVPVLATDTPEELAARVLHEEHQLYVEVVAALCEERIV 194
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
37-209 |
2.98e-26 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 102.49 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 37 LELLDAEKVQIVAVGS--DKD---------CPALERAQNLNIPTFRvPFDAvakKDREgwdirVLEAVNSFSPDIVVSAG 105
Cdd:COG0223 16 LEALLAAGHEVVAVVTqpDRPagrgrkltpSPVKELALEHGIPVLQ-PESL---KDPE-----FLEELRALNPDLIVVVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 106 FMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHE 185
Cdd:COG0223 87 YGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPIGPDDTAGSLHD 166
|
170 180
....*....|....*....|....
gi 2524658804 186 RIKVVERRLLVDVLHSIADHGIER 209
Cdd:COG0223 167 KLAELGAELLLETLDALEAGTLTP 190
|
|
| purU |
PRK06027 |
formyltetrahydrofolate deformylase; Reviewed |
16-213 |
5.57e-26 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 235676 [Multi-domain] Cd Length: 286 Bit Score: 101.34 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 16 SSKQLRIVVLAS----GLGSLL--QSMLELldaeKVQIVAVGSDKdcPALER-AQNLNIPTFRVPFDAVAKKDREGwdiR 88
Cdd:PRK06027 86 SAERKRVVILVSkedhCLGDLLwrWRSGEL----PVEIAAVISNH--DDLRSlVERFGIPFHHVPVTKETKAEAEA---R 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 89 VLEAVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILA 168
Cdd:PRK06027 157 LLELIDEYQPDLVVLARYMQILSPDFVARFPGRIINIHHSFLPAFKGAKPYHQAYERGVKLIGATAHYVTADLDEGPIIE 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2524658804 169 QQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRK 213
Cdd:PRK06027 237 QDVIRVDHRDTAEDLVRAGRDVEKQVLARAVRWHLEDRVLVYGNK 281
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
37-209 |
2.36e-24 |
|
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 95.20 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 37 LELLDAEKVQIVAVGS--DK---------DCPALERAQNLNIPTFRVPfdavAKKDREgwdirVLEAVNSFSPDIVVSAG 105
Cdd:cd08646 16 LEALLKSGHEVVAVVTqpDKprgrgkkltPSPVKELALELGLPVLQPE----KLKDEE-----FLEELKALKPDLIVVVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 106 FMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHE 185
Cdd:cd08646 87 YGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTAGELLD 166
|
170 180
....*....|....*....|....
gi 2524658804 186 RIKVVERRLLVDVLHSIADHGIER 209
Cdd:cd08646 167 KLAELGADLLLEVLDDIEAGKLNP 190
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
21-202 |
4.35e-23 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 91.56 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 21 RIVVLASGLGSLlqSMLELLDAEKVQIVAV--------GSD-KDCPALERAQNLNIPTFrvPFDAVAKKDregwdirVLE 91
Cdd:cd08651 1 RIVFIGCVEFSL--IALEAILEAGGEVVGVitlddsssNNDsDYLDLDSFARKNGIPYY--KFTDINDEE-------IIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 92 AVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQP 171
Cdd:cd08651 70 WIKEANPDIIFVFGWSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEP 149
|
170 180 190
....*....|....*....|....*....|.
gi 2524658804 172 VAVEDDDTVETLHERIKVVERRLLVDVLHSI 202
Cdd:cd08651 150 FPIDKDDTANSLYDKIMEAAKQQIDKFLPRL 180
|
|
| PRK13011 |
PRK13011 |
formyltetrahydrofolate deformylase; Reviewed |
15-213 |
7.67e-22 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 237266 [Multi-domain] Cd Length: 286 Bit Score: 90.43 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 15 SSSKQLRIVVLASGLGSLLQSML------ELldaeKVQIVAVGSDKdcPALER-AQNLNIPTFRVPFDAVAKKDREGwdi 87
Cdd:PRK13011 85 DPAARPKVLIMVSKFDHCLNDLLyrwrigEL----PMDIVGVVSNH--PDLEPlAAWHGIPFHHFPITPDTKPQQEA--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 88 RVLEAVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPIL 167
Cdd:PRK13011 156 QVLDVVEESGAELVVLARYMQVLSPELCRKLAGRAINIHHSFLPGFKGAKPYHQAYERGVKLIGATAHYVTDDLDEGPII 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2524658804 168 AQQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRK 213
Cdd:PRK13011 236 EQDVERVDHAYSPEDLVAKGRDVECLTLARAVKAHIERRVFLNGNR 281
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
20-204 |
1.19e-21 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 90.54 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLASGLGSLLQsmLELLDAEKVQIVAVGSDKDCPA-----------LERAQNLNIPTFRvpfDAVAKKDREGWDIR 88
Cdd:TIGR00460 1 LRIVFFGTPTFSLPV--LEELREDNFEVVGVVTQPDKPAgrgkkltpppvKVLAEEKGIPVFQ---PEKQRQLEELPLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 89 VLEavnsfsPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILA 168
Cdd:TIGR00460 76 ELK------PDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILK 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 2524658804 169 QQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIAD 204
Cdd:TIGR00460 150 QETFPIEEEDNSGTLSDKLSELGAQLLIETLKELPE 185
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
88-202 |
1.19e-18 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 78.79 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 88 RVLEAVNSFSPDIVVSAGfMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYG-VKVTGTTVHIVDNGVDTGPI 166
Cdd:cd08653 38 EVVAALRALAPDVVSVYG-CGIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGdPDNVGVTVHLVDAGIDTGDV 116
|
90 100 110
....*....|....*....|....*....|....*.
gi 2524658804 167 LAQQPVAVEDDDTVETLHERIKVVERRLLVDVLHSI 202
Cdd:cd08653 117 LAQARPPLAAGDTLLSLYLRLYRAGVELMVEAIADL 152
|
|
| purU |
PRK13010 |
formyltetrahydrofolate deformylase; Reviewed |
3-213 |
3.14e-18 |
|
formyltetrahydrofolate deformylase; Reviewed
Pssm-ID: 139334 [Multi-domain] Cd Length: 289 Bit Score: 81.00 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 3 EAQPVAE----ISHNNSSSKQLRIVVLASGLGSLLQSML--ELLDAEKVQIVAVGSDKdcPALER-AQNLNIPTFRVPfd 75
Cdd:PRK13010 73 EFQPVAEkfdmQWAIHPDGQRPKVVIMVSKFDHCLNDLLyrWRMGELDMDIVGIISNH--PDLQPlAVQHDIPFHHLP-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 76 aVAKKDREGWDIRVLEAVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVH 155
Cdd:PRK13010 149 -VTPDTKAQQEAQILDLIETSGAELVVLARYMQVLSDDLSRKLSGRAINIHHSFLPGFKGARPYHQAHARGVKLIGATAH 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658804 156 IVDNGVDTGPILAQQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRK 213
Cdd:PRK13010 228 FVTDDLDEGPIIEQDVERVDHSYSPEDLVAKGRDVECLTLARAVKAFIEHRVFINGDR 285
|
|
| PLN02828 |
PLN02828 |
formyltetrahydrofolate deformylase |
15-213 |
5.12e-18 |
|
formyltetrahydrofolate deformylase
Pssm-ID: 178422 Cd Length: 268 Bit Score: 79.79 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 15 SSSKQLRIVVLASGLGSLLQSMLELLDAEK--VQIVAVGSDKDcpaleRAQNLNIPTF----RVPFDAVAKKDREGWDIR 88
Cdd:PLN02828 66 GLDPKYKIAVLASKQDHCLIDLLHRWQDGRlpVDITCVISNHE-----RGPNTHVMRFlerhGIPYHYLPTTKENKREDE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 89 VLEAVNSfsPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILA 168
Cdd:PLN02828 141 ILELVKG--TDFLVLARYMQILSGNFLKGYGKDIINIHHGLLPSFKGGNPSKQAFDAGVKLIGATSHFVTEELDAGPIIE 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2524658804 169 QQPVAVEDDDTVETLHERIKVVERRLLVDVLHSIADHGIERDGRK 213
Cdd:PLN02828 219 QMVERVSHRDNLRSFVQKSENLEKQCLAKAIKSYCELRVLPYGTN 263
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
57-214 |
1.51e-15 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 73.96 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 57 PALERAQNLNIPTFRVpfdAVAKKDREGWDIRVLEAVNsfsPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGA 136
Cdd:PLN02285 59 PVAQLALDRGFPPDLI---FTPEKAGEEDFLSALRELQ---PDLCITAAYGNILPQKFLDIPKLGTVNIHPSLLPLYRGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 137 RAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHERIKVVERRLLVDVLHSI-----ADHGIERDG 211
Cdd:PLN02285 133 APVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPLLFELGTKLLLRELPSVldgsaKDKATPQDD 212
|
...
gi 2524658804 212 RKA 214
Cdd:PLN02285 213 SKA 215
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
20-214 |
1.51e-15 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 71.72 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 20 LRIVVLasGLGSLLQSMLELLDAEKVQIVAV----GSDKDCPALERAQNLNIPTFRVPFDAvAKKDREGwdirvleavns 95
Cdd:cd08822 1 MKIAIA--GQKWFGTAVLEALRARGIALLGVaapeEGDRLAAAARTAGSRGLPRAGVAVLP-ADAIPPG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 96 fsPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVE 175
Cdd:cd08822 67 --TDLIVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2524658804 176 DDDTVETLHER-IKVVERRLLVDVLHSIADHG----IERDGRKA 214
Cdd:cd08822 145 PGDTAAELWRRaLAPMGVKLLTQVIDALLRGGnlpaQPQDERLA 188
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
37-195 |
7.33e-13 |
|
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.
Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 64.67 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 37 LELLDAEKVQIVAVGSDKDCPA--------LERAQNLNIPTFRvPFDAvakKDREGwdirvLEAVNSFSPDIVVSAGFMR 108
Cdd:cd08644 16 LEALLAAGFEVVAVFTHTDNPGeniwfgsvAQLAREHGIPVFT-PDDI---NHPEW-----VERLRALKPDLIFSFYYRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 109 ILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHERIK 188
Cdd:cd08644 87 MISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLC 166
|
....*..
gi 2524658804 189 VVERRLL 195
Cdd:cd08644 167 VAARRLL 173
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
22-199 |
2.49e-12 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 62.85 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 22 IVVLASGlgSLLQSMLELLDAE-KVQIVAVgsdkdcPALERAQNLNIPTFRVPFDAVAKK--DREGWDIRVLEAVNSFSP 98
Cdd:cd08823 1 IVILCNT--SMAAPLLGQLLSEgRLAGIAV------PAHNASYFPQIFVFTGIRRLVSKQrvDTANLKEQLAEWLRALAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 99 DIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDD 178
Cdd:cd08823 73 DTVVVFTFPYRIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDD 152
|
170 180
....*....|....*....|.
gi 2524658804 179 TVETLHERIkvveRRLLVDVL 199
Cdd:cd08823 153 TYGLLCSRL----AMLAVGLL 169
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
33-185 |
2.85e-12 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 62.46 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 33 LQSMLELLDAEKVQIVAVGSDkdcpalerAQNLNIPTFRVPFDAVAKKDREgwDIRVLEAVNSFSPDIVVSAGFMRILGP 112
Cdd:cd08820 15 LRTLLRLQDRGSFEIIAVLTN--------TSPADVWEGSEPLYDIGSTERN--LHKLLEILENKGVDILISVQYHWILPG 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524658804 113 SFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHE 185
Cdd:cd08820 85 SILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVISLYI 157
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
90-203 |
4.31e-12 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 64.62 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 90 LEAVNSFSPDIVVSAGFMRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQ 169
Cdd:PRK08125 68 VERIRELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQ 147
|
90 100 110
....*....|....*....|....*....|....
gi 2524658804 170 QPVAVEDDDTVETLHERIKVVERRLLVDVLHSIA 203
Cdd:PRK08125 148 QRVAIAPDDTALTLHHKLCHAARQLLEQTLPAIK 181
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
44-186 |
2.07e-11 |
|
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.
Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 60.93 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 44 KVQIVAVGSDKD-CPALE----RAQNLNIPtfrvpfDAVAKKDREGWDIRVLEAVNSFSPdivvsagfMRIlgpsfVEAY 118
Cdd:cd08647 38 KADPLALEAEKDgVPVFKfprwRAKGQAIP------EVVAKYKALGAELNVLPFCSQFIP--------MEV-----IDAP 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524658804 119 SNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHER 186
Cdd:cd08647 99 KHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTVDTLYNR 166
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
28-183 |
2.09e-08 |
|
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.
Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 51.88 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 28 GLGSLLQSMLELLDAEKVQIVAVGSDKdcPALER-AQNLNIPTFRVPFDAvakkdregwdirvLEAVNSFSPDIVVSAGF 106
Cdd:cd08649 6 GGGTLLIQCAEQLLAAGHRIAAVVSTD--PAIRAwAAAEGIAVLEPGEAL-------------EELLSDEPFDWLFSIVN 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524658804 107 MRILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETL 183
Cdd:cd08649 71 LRILPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
121-204 |
2.34e-08 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 52.60 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 121 RIINTHPALLPS----FPGARAVPDALDYGVkvtgtTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHERIKVVERRLLV 196
Cdd:PRK07579 87 RCINIHPGFNPYnrgwFPQVFSIINGLKIGA-----TIHEMDEQLDHGPIIAQREVEIESWDSSGSVYARVMDIERELVL 161
|
....*...
gi 2524658804 197 DVLHSIAD 204
Cdd:PRK07579 162 EHFDAIRD 169
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
37-199 |
6.77e-07 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 48.92 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 37 LELLDAEKVQIVAVGSDKDCPA--------LERAQNLNIPtFRVPFDAVakkdregwDIRVLEAVNSFSPDIVVSAGFMR 108
Cdd:PRK06988 18 LQVLLARGVDVALVVTHEDNPTeniwfgsvAAVAAEHGIP-VITPADPN--------DPELRAAVAAAAPDFIFSFYYRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524658804 109 ILGPSFVEAYSNRIINTHPALLPSFPGARAVPDALDYGVKVTGTTVHIVDNGVDTGPILAQQPVAVEDDDTVETLHERIK 188
Cdd:PRK06988 89 MIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFDKVT 168
|
170
....*....|.
gi 2524658804 189 VVERRLLVDVL 199
Cdd:PRK06988 169 VAAEQTLWRVL 179
|
|
| |
